Maria Anne Schumacher | Scholars@Duke

Maria Anne Schumacher
Nanaline H. Duke Distinguished Professor of Biochemistry

Current Appointments & Affiliations

Nanaline H. Duke Distinguished Professor of Biochemistry, Biochemistry, Basic Science Departments 2017
Professor of Biochemistry, Biochemistry, Basic Science Departments 2015

Contact Information

243A Nanaline H Duke, Durham, NC 27710
Box 3711, Durham, NC 27710
maria.schumacher@duke.edu (919) 684-9468

Background
Education, Training, & Certifications
- Ph.D., Oregon Health and Science University 1995
Duke Appointment History
- Associate Professor of Biochemistry, Biochemistry, Basic Science Departments 2011 - 2015
- Instructor in the Department of Biochemistry, Biochemistry, Basic Science Departments 2011
Recognition
In the News
- FEB 10, 2021
  
  Duke Celebrates Women and Girls in Science Day
- NOV 19, 2020
  
  Researchers Peer Inside Deadly Pathogen’s Burglary Kit
- OCT 21, 2020
  
  Transcription Factors May Inadvertently Lock in DNA Mistakes
- SEP 6, 2017
  
  Molecular Map Shows How to Disable Dangerous Bioweapon
- JUL 29, 2015
  
  Structures Reveal Basis of Recurring Urinary Tract Infections
- MAR 10, 2015
  
  Schumacher elected to American Academy of Microbiology
- AUG 28, 2014
  
  Small Molecule Acts As On-Off Switch for Nature's Antibiotic Factory
- JUN 9, 2014
  
  Protein Could Put Antibiotic-Resistant Bugs in Handcuffs
Awards & Honors
- AAAS Fellows. American Association for the Advancement of Science, The. 2012
Research
Selected Grants
- Biosynthesis of antifungal nucleoside antibiotics awarded by National Institutes of Health 2015 - 2024
- Mechanism of carbon skeleton formation in molybdenum cofactor biosynthesis awarded by National Institutes of Health 2015 - 2024
- Deciphering fundamental biological processes involving protein-nucleic acid interactions at the molecular level awarded by National Institutes of Health 2019 - 2023
- Mechanistic Insights into m6A-Mediated Regulation of Brain Development awarded by National Institutes of Health 2018 - 2023
- Structural studies of virulence activation in Francisella tularensis awarded by National Institutes of Health 2020 - 2023
- Structural Elucidation of the Novel RNA Polymerase Underlying Francisella Tularensis Virulence awarded by National Institutes of Health 2020 - 2022
- Organization and Function of Cellular Structure awarded by National Institutes of Health 1975 - 2020
- Complete atomic dissection of the B. subtilis nitrogen regulatory pathway awarded by National Institutes of Health 2015 - 2020
- Assembly and partition mechanism of Walker-box based segregation machinery awarded by National Institutes of Health 2015 - 2019
- Structural Biology and Biophysics Training Program awarded by National Institutes of Health 1994 - 2015
- Structural mechanism of DNA segregation by the pSK41 par system awarded by National Institutes of Health 2009 - 2012
Publications & Artistic Works
Selected Publications
- Academic Articles
  - Travis, Brady A., Kathryn M. Ramsey, Samantha M. Prezioso, Thomas Tallo, Jamie M. Wandzilak, Allen Hsu, Mario Borgnia, et al. “Structural Basis for Virulence Activation of Francisella tularensis.” Mol Cell 81, no. 1 (January 7, 2021): 139-152.e10. https://doi.org/10.1016/j.molcel.2020.10.035.
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  - Afek, Ariel, Honglue Shi, Atul Rangadurai, Harshit Sahay, Alon Senitzki, Suela Xhani, Mimi Fang, et al. “DNA mismatches reveal conformational penalties in protein-DNA recognition.” Nature 587, no. 7833 (November 2020): 291–96. https://doi.org/10.1038/s41586-020-2843-2.
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  - Dorman, Charles J., Maria A. Schumacher, Matthew J. Bush, Richard G. Brennan, and Mark J. Buttner. “When is a transcription factor a NAP?” Curr Opin Microbiol 55 (June 2020): 26–33. https://doi.org/10.1016/j.mib.2020.01.019.
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  - Gallagher, Kelley A., Maria A. Schumacher, Matthew J. Bush, Maureen J. Bibb, Govind Chandra, Neil A. Holmes, Wenjie Zeng, et al. “c-di-GMP Arms an Anti-σ to Control Progression of Multicellular Differentiation in Streptomyces.” Mol Cell 77, no. 3 (February 6, 2020): 586-599.e6. https://doi.org/10.1016/j.molcel.2019.11.006.
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  - Schumacher, Maria A., Max Henderson, and Wenjie Zeng. “Structures of MERS1, the 5' processing enzyme of mitochondrial mRNAs in Trypanosoma brucei.” Rna 26, no. 1 (January 2020): 69–82. https://doi.org/10.1261/rna.072231.119.
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  - Juvvadi, Praveen R., David Fox, Benjamin G. Bobay, Michael J. Hoy, Sophie M. C. Gobeil, Ronald A. Venters, Zanetta Chang, et al. “Harnessing calcineurin-FK506-FKBP12 crystal structures from invasive fungal pathogens to develop antifungal agents.” Nat Commun 10, no. 1 (September 19, 2019): 4275. https://doi.org/10.1038/s41467-019-12199-1.
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  - Stelling, Allison L., Amy Y. Liu, Wenjie Zeng, Raul Salinas, Maria A. Schumacher, and Hashim M. Al-Hashimi. “Infrared Spectroscopic Observation of a G-C+ Hoogsteen Base Pair in the DNA:TATA-Box Binding Protein Complex Under Solution Conditions.” Angew Chem Int Ed Engl 58, no. 35 (August 26, 2019): 12010–13. https://doi.org/10.1002/anie.201902693.
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  - Schumacher, Maria A., Max Henderson, and Hengshan Zhang. “Structures of maintenance of carboxysome distribution Walker-box McdA and McdB adaptor homologs.” Nucleic Acids Res 47, no. 11 (June 20, 2019): 5950–62. https://doi.org/10.1093/nar/gkz314.
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  - Travis, Brady, Porsha L. R. Shaw, Bei Liu, Krishna Ravindra, Hadley Iliff, Hashim M. Al-Hashimi, and Maria A. Schumacher. “The RRM of the kRNA-editing protein TbRGG2 uses multiple surfaces to bind and remodel RNA.” Nucleic Acids Res 47, no. 4 (February 28, 2019): 2130–42. https://doi.org/10.1093/nar/gky1259.
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  - Guo, Monica S., Diane L. Haakonsen, Wenjie Zeng, Maria A. Schumacher, and Michael T. Laub. “A Bacterial Chromosome Structuring Protein Binds Overtwisted DNA to Stimulate Type II Topoisomerases and Enable DNA Replication.” Cell 175, no. 2 (October 4, 2018): 583-597.e23. https://doi.org/10.1016/j.cell.2018.08.029.
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  - Schumacher, Maria A., Matthew J. Bush, Maureen J. Bibb, Félix Ramos-León, Govind Chandra, Wenjie Zeng, and Mark J. Buttner. “The crystal structure of the RsbN-σBldN complex from Streptomyces venezuelae defines a new structural class of anti-σ factor.” Nucleic Acids Res 46, no. 14 (August 21, 2018): 7405–17. https://doi.org/10.1093/nar/gky493.
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  - Schumacher, Maria A., Matthew J. Bush, Maureen J. Bibb, Félix Ramos-León, Govind Chandra, Wenjie Zeng, and Mark J. Buttner. “The crystal structure of the RsbN-σBldN complex from Streptomyces venezuelae defines a new structural class of anti-σ factor.” Nucleic Acids Res 46, no. 14 (August 21, 2018): 7467–68. https://doi.org/10.1093/nar/gky616.
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  - Liu, Bei, Dawn K. Merriman, Seung H. Choi, Maria A. Schumacher, Raphael Plangger, Christoph Kreutz, Stacy M. Horner, Kate D. Meyer, and Hashim M. Al-Hashimi. “A potentially abundant junctional RNA motif stabilized by m6A and Mg2.” Nat Commun 9, no. 1 (July 17, 2018): 2761. https://doi.org/10.1038/s41467-018-05243-z.
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  - Toleman, Clifford A., Maria A. Schumacher, Seok-Ho Yu, Wenjie Zeng, Nathan J. Cox, Timothy J. Smith, Erik J. Soderblom, Amberlyn M. Wands, Jennifer J. Kohler, and Michael Boyce. “Structural basis of O-GlcNAc recognition by mammalian 14-3-3 proteins.” Proc Natl Acad Sci U S A 115, no. 23 (June 5, 2018): 5956–61. https://doi.org/10.1073/pnas.1722437115.
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  - Schumacher, Maria A., Chris D. den Hengst, Matthew J. Bush, T. B. K. Le, Ngat T. Tran, Govind Chandra, Wenjie Zeng, Brady Travis, Richard G. Brennan, and Mark J. Buttner. “The MerR-like protein BldC binds DNA direct repeats as cooperative multimers to regulate Streptomyces development.” Nat Commun 9, no. 1 (March 19, 2018): 1139. https://doi.org/10.1038/s41467-018-03576-3.
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  - Cuthbert, Bonnie J., Wilma Ross, Amy E. Rohlfing, Simon L. Dove, Richard L. Gourse, Richard G. Brennan, and Maria A. Schumacher. “Dissection of the molecular circuitry controlling virulence in Francisella tularensis.” Genes Dev 31, no. 15 (August 1, 2017): 1549–60. https://doi.org/10.1101/gad.303701.117.
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  - Schumacher, Maria A., Wenjie Zeng, Kim C. Findlay, Mark J. Buttner, Richard G. Brennan, and Natalia Tschowri. “The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD2-(c-di-GMP)4 complex.” Nucleic Acids Res 45, no. 11 (June 20, 2017): 6923–33. https://doi.org/10.1093/nar/gkx287.
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  - McLeod, Brett N., Gina E. Allison-Gamble, Madhuri T. Barge, Nam K. Tonthat, Maria A. Schumacher, Finbarr Hayes, and Daniela Barillà. “A three-dimensional ParF meshwork assembles through the nucleoid to mediate plasmid segregation.” Nucleic Acids Res 45, no. 6 (April 7, 2017): 3158–71. https://doi.org/10.1093/nar/gkw1302.
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  - Schumacher, Maria A., Kuo-Hsiang Huang, Wenjie Zeng, and Anuradha Janakiraman. “Structure of the Z Ring-associated Protein, ZapD, Bound to the C-terminal Domain of the Tubulin-like Protein, FtsZ, Suggests Mechanism of Z Ring Stabilization through FtsZ Cross-linking.” J Biol Chem 292, no. 9 (March 3, 2017): 3740–50. https://doi.org/10.1074/jbc.M116.773192.
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  - Zhang, Hengshan, and Maria A. Schumacher. “Structures of partition protein ParA with nonspecific DNA and ParB effector reveal molecular insights into principles governing Walker-box DNA segregation.” Genes Dev 31, no. 5 (March 1, 2017): 481–92. https://doi.org/10.1101/gad.296319.117.
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  - Schumacher, Maria A. “Bacterial Nucleoid Occlusion: Multiple Mechanisms for Preventing Chromosome Bisection During Cell Division.” Subcell Biochem 84 (2017): 267–98. https://doi.org/10.1007/978-3-319-53047-5_9.
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  - Schumacher, Maria A., and Wenjie Zeng. “Structures of the activator of K. pneumonia biofilm formation, MrkH, indicates PilZ domains involved in c-di-GMP and DNA binding.” Proc Natl Acad Sci U S A 113, no. 36 (September 6, 2016): 10067–72. https://doi.org/10.1073/pnas.1607503113.
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  - Schumacher, Maria A., Jeehyun Lee, and Wenjie Zeng. “Molecular insights into DNA binding and anchoring by the Bacillus subtilis sporulation kinetochore-like RacA protein.” Nucleic Acids Res 44, no. 11 (June 20, 2016): 5438–49. https://doi.org/10.1093/nar/gkw248.
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  - Schumacher, Maria A., and Wenjie Zeng. “Structures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ.” Proc Natl Acad Sci U S A 113, no. 18 (May 3, 2016): 4988–93. https://doi.org/10.1073/pnas.1602327113.
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  - Tonthat, Nam K., Praveen Rao Juvvadi, Hengshan Zhang, Soo Chan Lee, Ron Venters, Leonard Spicer, William J. Steinbach, Joseph Heitman, and Maria A. Schumacher. “Structures of Pathogenic Fungal FKBP12s Reveal Possible Self-Catalysis Function.” Mbio 7, no. 2 (April 26, 2016): e00492–e00416. https://doi.org/10.1128/mBio.00492-16.
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  - Schumacher, Maria A., Wenjie Zeng, Kuo-Hsiang Huang, Lukasz Tchorzewski, and Anuradha Janakiraman. “Structural and Functional Analyses Reveal Insights into the Molecular Properties of the Escherichia coli Z Ring Stabilizing Protein, ZapC.” J Biol Chem 291, no. 5 (January 29, 2016): 2485–98. https://doi.org/10.1074/jbc.M115.697037.
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  - Schumacher, Maria A., Nam K. Tonthat, Jeehyun Lee, Fernando A. Rodriguez-Castañeda, Naga Babu Chinnam, Anne K. Kalliomaa-Sanford, Irene W. Ng, Madhuri T. Barge, Porsha L. R. Shaw, and Daniela Barillà. “Structures of archaeal DNA segregation machinery reveal bacterial and eukaryotic linkages.” Science 349, no. 6252 (September 4, 2015): 1120–24. https://doi.org/10.1126/science.aaa9046.
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  - Lee, Soo Chan, Alicia Li, Silvia Calo, Makoto Inoue, Nam K. Tonthat, Judith M. Bain, Johanna Louw, et al. “Calcineurin orchestrates dimorphic transitions, antifungal drug responses and host-pathogen interactions of the pathogenic mucoralean fungus Mucor circinelloides.” Mol Microbiol 97, no. 5 (September 2015): 844–65. https://doi.org/10.1111/mmi.13071.
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  - Shaw, Porsha L. R., Natalie M. McAdams, Michael A. Hast, Michelle L. Ammerman, Laurie K. Read, and Maria A. Schumacher. “Structures of the T. brucei kRNA editing factor MRB1590 reveal unique RNA-binding pore motif contained within an ABC-ATPase fold.” Nucleic Acids Res 43, no. 14 (August 18, 2015): 7096–7109. https://doi.org/10.1093/nar/gkv647.
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  - Schumacher, Maria A., Pooja Balani, Jungki Min, Naga Babu Chinnam, Sonja Hansen, Marin Vulić, Kim Lewis, and Richard G. Brennan. “HipBA-promoter structures reveal the basis of heritable multidrug tolerance.” Nature 524, no. 7563 (August 6, 2015): 59–64. https://doi.org/10.1038/nature14662.
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  - Hover, Bradley M., Nam K. Tonthat, Maria A. Schumacher, and Kenichi Yokoyama. “Mechanism of pyranopterin ring formation in molybdenum cofactor biosynthesis.” Proc Natl Acad Sci U S A 112, no. 20 (May 19, 2015): 6347–52. https://doi.org/10.1073/pnas.1500697112.
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  - Schumacher, Maria A., Naga Babu Chinnam, Bonnie Cuthbert, Nam K. Tonthat, and Travis Whitfill. “Structures of regulatory machinery reveal novel molecular mechanisms controlling B. subtilis nitrogen homeostasis.” Genes Dev 29, no. 4 (February 15, 2015): 451–64. https://doi.org/10.1101/gad.254714.114.
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  - Cuthbert, Bonnie J., Richard G. Brennan, and Maria A. Schumacher. “Structural and Biochemical Characterization of the Francisella tularensis Pathogenicity Regulator, Macrophage Locus Protein A (MglA).” Plos One 10, no. 6 (2015): e0128225. https://doi.org/10.1371/journal.pone.0128225.
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  - Emptage, Ryan P., Nam K. Tonthat, John D. York, Maria A. Schumacher, and Pei Zhou. “Structural basis of lipid binding for the membrane-embedded tetraacyldisaccharide-1-phosphate 4'-kinase LpxK.” J Biol Chem 289, no. 35 (August 29, 2014): 24059–68. https://doi.org/10.1074/jbc.M114.589986.
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  - Tschowri, Natalia, Maria A. Schumacher, Susan Schlimpert, Naga Babu Chinnam, Kim C. Findlay, Richard G. Brennan, and Mark J. Buttner. “Tetrameric c-di-GMP mediates effective transcription factor dimerization to control Streptomyces development.” Cell 158, no. 5 (August 28, 2014): 1136–47. https://doi.org/10.1016/j.cell.2014.07.022.
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  - Schumacher, Maria A., Nam K. Tonthat, Stephen M. Kwong, Naga Babu Chinnam, Michael A. Liu, Ronald A. Skurray, and Neville Firth. “Mechanism of staphylococcal multiresistance plasmid replication origin assembly by the RepA protein.” Proc Natl Acad Sci U S A 111, no. 25 (June 24, 2014): 9121–26. https://doi.org/10.1073/pnas.1406065111.
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  - Daniels, Kyle G., Nam K. Tonthat, David R. McClure, Yu-Chu Chang, Xin Liu, Maria A. Schumacher, Carol A. Fierke, Scott C. Schmidler, and Terrence G. Oas. “Ligand concentration regulates the pathways of coupled protein folding and binding.” J Am Chem Soc 136, no. 3 (January 22, 2014): 822–25. https://doi.org/10.1021/ja4086726.
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  - Murray, David S., Nagababu Chinnam, Nam Ky Tonthat, Travis Whitfill, Lewis V. Wray, Susan H. Fisher, and Maria A. Schumacher. “Structures of the Bacillus subtilis glutamine synthetase dodecamer reveal large intersubunit catalytic conformational changes linked to a unique feedback inhibition mechanism.” J Biol Chem 288, no. 50 (December 13, 2013): 35801–11. https://doi.org/10.1074/jbc.M113.519496.
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  - Schumacher, Maria A., Nagababu Chinnam, Tomoo Ohashi, Riddhi Sanjay Shah, and Harold P. Erickson. “The structure of irisin reveals a novel intersubunit β-sheet fibronectin type III (FNIII) dimer: implications for receptor activation.” J Biol Chem 288, no. 47 (November 22, 2013): 33738–44. https://doi.org/10.1074/jbc.M113.516641.
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  - Tonthat, N. K., S. L. Milam, N. Chinnam, T. Whitfill, W. Margolin, and M. A. Schumacher. “Erratum: SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid (Proceedings of the National Academy of Sciences of the United States of America (2013) 110, 26, (10586-10591) DOI: 10.1073/pnas.1221036110).” Proceedings of the National Academy of Sciences of the United States of America 110, no. 37 (September 10, 2013): 15163. https://doi.org/10.1073/pnas.1314545110.
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  - Tonthat, Nam K., Sara L. Milam, Nagababu Chinnam, Travis Whitfill, William Margolin, and Maria A. Schumacher. “SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid.” Proc Natl Acad Sci U S A 110, no. 26 (June 25, 2013): 10586–91. https://doi.org/10.1073/pnas.1221036110.
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  - Ni, Lisheng, Nam K. Tonthat, Nagababu Chinnam, and Maria A. Schumacher. “Structures of the Escherichia coli transcription activator and regulator of diauxie, XylR: an AraC DNA-binding family member with a LacI/GalR ligand-binding domain.” Nucleic Acids Res 41, no. 3 (February 1, 2013): 1998–2008. https://doi.org/10.1093/nar/gks1207.
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  - Dobruk-Serkowska, Aneta, Marisa Caccamo, Fernando Rodríguez-Castañeda, Meiyi Wu, Kerstyn Bryce, Irene Ng, Maria A. Schumacher, Daniela Barillà, and Finbarr Hayes. “Uncoupling of nucleotide hydrolysis and polymerization in the ParA protein superfamily disrupts DNA segregation dynamics.” J Biol Chem 287, no. 51 (December 14, 2012): 42545–53. https://doi.org/10.1074/jbc.M112.410324.
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  - Dupaigne, Pauline, Nam K. Tonthat, Olivier Espéli, Travis Whitfill, Frédéric Boccard, and Maria A. Schumacher. “Molecular basis for a protein-mediated DNA-bridging mechanism that functions in condensation of the E. coli chromosome.” Mol Cell 48, no. 4 (November 30, 2012): 560–71. https://doi.org/10.1016/j.molcel.2012.09.009.
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  - Schumacher, Maria A., JungKi Min, Todd M. Link, Ziqiang Guan, Weijun Xu, Young-Ho Ahn, Erik J. Soderblom, et al. “Role of unusual P loop ejection and autophosphorylation in HipA-mediated persistence and multidrug tolerance.” Cell Reports 2, no. 3 (September 20, 2012): 518–25. https://doi.org/10.1016/j.celrep.2012.08.013.
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  - Schumacher, Maria A., Qiaozhen Ye, Madhuri T. Barge, Massimiliano Zampini, Daniela Barillà, and Finbarr Hayes. “Structural mechanism of ATP-induced polymerization of the partition factor ParF: implications for DNA segregation.” J Biol Chem 287, no. 31 (July 27, 2012): 26146–54. https://doi.org/10.1074/jbc.M112.373696.
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  - Schumacher, Maria A. “Bacterial plasmid partition machinery: a minimalist approach to survival.” Curr Opin Struct Biol 22, no. 1 (February 2012): 72–79. https://doi.org/10.1016/j.sbi.2011.11.001.
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  - Hansen, Sonja, Marin Vulić, Jungki Min, Tien-Jui Yen, Maria A. Schumacher, Richard G. Brennan, and Kim Lewis. “Regulation of the Escherichia coli HipBA toxin-antitoxin system by proteolysis.” Plos One 7, no. 6 (2012): e39185. https://doi.org/10.1371/journal.pone.0039185.
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  - Le, Tung B. K., Maria A. Schumacher, David M. Lawson, Richard G. Brennan, and Mark J. Buttner. “The crystal structure of the TetR family transcriptional repressor SimR bound to DNA and the role of a flexible N-terminal extension in minor groove binding.” Nucleic Acids Res 39, no. 21 (November 2011): 9433–47. https://doi.org/10.1093/nar/gkr640.
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  - Takeda, Kojiro, Nam K. Tonthat, Tiffany Glover, Weijun Xu, Eugene V. Koonin, Mitsuhiro Yanagida, and Maria A. Schumacher. “Implications for proteasome nuclear localization revealed by the structure of the nuclear proteasome tether protein Cut8.” Proceedings of the National Academy of Sciences of the United States of America 108, no. 41 (October 5, 2011): 16950–55. https://doi.org/10.1073/pnas.1103617108.
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  - Gu, Dongmin, Nam Ky Tonthat, Moonsup Lee, Hong Ji, Krishna P. Bhat, Faith Hollingsworth, Kenneth D. Aldape, Maria A. Schumacher, Thomas P. Zwaka, and Pierre D. McCrea. “Caspase-3 cleavage links delta-catenin to the novel nuclear protein ZIFCAT.” J Biol Chem 286, no. 26 (July 1, 2011): 23178–88. https://doi.org/10.1074/jbc.M110.167544.
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  - Schumacher, Maria A., Mareen Sprehe, Maike Bartholomae, Wolfgang Hillen, and Richard G. Brennan. “Structures of carbon catabolite protein A-(HPr-Ser46-P) bound to diverse catabolite response element sites reveal the basis for high-affinity binding to degenerate DNA operators.” Nucleic Acids Research 39, no. 7 (April 2011): 2931–42. https://doi.org/10.1093/nar/gkq1177.
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  - Peters, Kate M., Benjamin E. Brooks, Maria A. Schumacher, Ronald A. Skurray, Richard G. Brennan, and Melissa H. Brown. “A single acidic residue can guide binding site selection but does not govern QacR cationic-drug affinity.” Plos One 6, no. 1 (January 17, 2011): e15974. https://doi.org/10.1371/journal.pone.0015974.
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  - Tonthat, Nam Ky, Stefan T. Arold, Brian F. Pickering, Michael W. Van Dyke, Shoudan Liang, Yue Lu, Tushar K. Beuria, William Margolin, and Maria A. Schumacher. “Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check.” Embo J 30, no. 1 (January 5, 2011): 154–64. https://doi.org/10.1038/emboj.2010.288.
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  - Schumacher, Maria A., Kevin M. Piro, and Weijun Xu. “Insight into F plasmid DNA segregation revealed by structures of SopB and SopB-DNA complexes.” Nucleic Acids Res 38, no. 13 (July 2010): 4514–26. https://doi.org/10.1093/nar/gkq161.
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  - Ni, Lisheng, Weijun Xu, Muthiah Kumaraswami, and Maria A. Schumacher. “Plasmid protein TubR uses a distinct mode of HTH-DNA binding and recruits the prokaryotic tubulin homolog TubZ to effect DNA partition.” Proc Natl Acad Sci U S A 107, no. 26 (June 29, 2010): 11763–68. https://doi.org/10.1073/pnas.1003817107.
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  - Sprehe, Mareen, John C. Fisk, Sarah M. McEvoy, Laurie K. Read, and Maria A. Schumacher. “Structure of the Trypanosoma brucei p22 protein, a cytochrome oxidase subunit II-specific RNA-editing accessory factor.” J Biol Chem 285, no. 24 (June 11, 2010): 18899–908. https://doi.org/10.1074/jbc.M109.066597.
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  - Popp, D., W. Xu, A. Narita, A. J. Brzoska, R. A. Skurray, N. Firth, U. Ghoshdastider, Y. Maéda, R. C. Robinson, and M. A. Schumacher. “Erratum: Structure and filament dynamics of the pSK41 actin-like ParM protein. Implications for plasmid DNA segregation (Journal of Biological Chemistry (2010) 285, (10130-10140) DOI: 10.1074/jbc.A109.071613).” Journal of Biological Chemistry 285, no. 23 (June 4, 2010): 18122.
  - Popp, David, Weijun Xu, Akihiro Narita, Anthony J. Brzoska, Ronald A. Skurray, Neville Firth, Umesh Ghoshdastider, Yuichiro Maéda, Robert C. Robinson, and Maria A. Schumacher. “Structure and filament dynamics of the pSK41 actin-like ParM protein: implications for plasmid DNA segregation.” J Biol Chem 285, no. 13 (March 26, 2010): 10130–40. https://doi.org/10.1074/jbc.M109.071613.
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  - Ni, Lisheng, Slade O. Jensen, Nam Ky Tonthat, Tracey Berg, Stephen M. Kwong, Fiona H. X. Guan, Melissa H. Brown, Ronald A. Skurray, Neville Firth, and Maria A. Schumacher. “The Staphylococcus aureus pSK41 plasmid-encoded ArtA protein is a master regulator of plasmid transmission genes and contains a RHH motif used in alternate DNA-binding modes.” Nucleic Acids Res 37, no. 20 (November 2009): 6970–83. https://doi.org/10.1093/nar/gkp756.
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  - Dunham, Thomas D., Weijun Xu, Barbara E. Funnell, and Maria A. Schumacher. “Structural basis for ADP-mediated transcriptional regulation by P1 and P7 ParA.” Embo J 28, no. 12 (June 17, 2009): 1792–1802. https://doi.org/10.1038/emboj.2009.120.
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  - Schumacher, Maria A., Kevin M. Piro, Weijun Xu, Sonja Hansen, Kim Lewis, and Richard G. Brennan. “Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB.” Science 323, no. 5912 (January 16, 2009): 396–401. https://doi.org/10.1126/science.1163806.
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  - Boudko, Sergei P., Jürgen Engel, Kenji Okuyama, Kazunori Mizuno, Hans Peter Bächinger, and Maria A. Schumacher. “Crystal structure of human type III collagen Gly991-Gly1032 cystine knot-containing peptide shows both 7/2 and 10/3 triple helical symmetries.” J Biol Chem 283, no. 47 (November 21, 2008): 32580–89. https://doi.org/10.1074/jbc.M805394200.
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  - Peters, Kate M., Jason T. Schuman, Ronald A. Skurray, Melissa H. Brown, Richard G. Brennan, and Maria A. Schumacher. “QacR-cation recognition is mediated by a redundancy of residues capable of charge neutralization.” Biochemistry 47, no. 31 (August 5, 2008): 8122–29. https://doi.org/10.1021/bi8008246.
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  - Zíková, Alena, Jana Kopecná, Maria A. Schumacher, Kenneth Stuart, Lukás Trantírek, and Julius Lukes. “Structure and function of the native and recombinant mitochondrial MRP1/MRP2 complex from Trypanosoma brucei.” Int J Parasitol 38, no. 8–9 (July 2008): 901–12. https://doi.org/10.1016/j.ijpara.2007.12.009.
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  - Schumacher, Maria A. “Structural biology of plasmid partition: uncovering the molecular mechanisms of DNA segregation.” Biochem J 412, no. 1 (May 15, 2008): 1–18. https://doi.org/10.1042/BJ20080359.
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  - Wilkinson, Deepti Srinivas, Wen-Wei Tsai, Maria A. Schumacher, and Michelle Craig Barton. “Chromatin-bound p53 anchors activated Smads and the mSin3A corepressor to confer transforming-growth-factor-beta-mediated transcription repression.” Mol Cell Biol 28, no. 6 (March 2008): 1988–98. https://doi.org/10.1128/MCB.01442-07.
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  - Schumacher, Maria A., Tiffany C. Glover, Anthony J. Brzoska, Slade O. Jensen, Thomas D. Dunham, Ronald A. Skurray, and Neville Firth. “Segrosome structure revealed by a complex of ParR with centromere DNA.” Nature 450, no. 7173 (December 20, 2007): 1268–71. https://doi.org/10.1038/nature06392.
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  - Schumacher, Maria A., Gerald Seidel, Wolfgang Hillen, and Richard G. Brennan. “Structural mechanism for the fine-tuning of CcpA function by the small molecule effectors glucose 6-phosphate and fructose 1,6-bisphosphate.” Journal of Molecular Biology 368, no. 4 (May 2007): 1042–50. https://doi.org/10.1016/j.jmb.2007.02.054.
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  - Vecchiarelli, Anthony G., Maria A. Schumacher, and Barbara E. Funnell. “P1 partition complex assembly involves several modes of protein-DNA recognition.” J Biol Chem 282, no. 15 (April 13, 2007): 10944–52. https://doi.org/10.1074/jbc.M611250200.
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  - Schumacher, Maria A., André Mansoor, and Barbara E. Funnell. “Structure of a four-way bridged ParB-DNA complex provides insight into P1 segrosome assembly.” J Biol Chem 282, no. 14 (April 6, 2007): 10456–64. https://doi.org/10.1074/jbc.M610603200.
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  - Schumacher, Maria A. “Structural biology of plasmid segregation proteins.” Curr Opin Struct Biol 17, no. 1 (February 2007): 103–9. https://doi.org/10.1016/j.sbi.2006.11.005.
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  - Schumacher, Maria A., Kazunori Mizuno, and Hans Peter Bächinger. “The crystal structure of a collagen-like polypeptide with 3(S)-hydroxyproline residues in the Xaa position forms a standard 7/2 collagen triple helix.” J Biol Chem 281, no. 37 (September 15, 2006): 27566–74. https://doi.org/10.1074/jbc.M602797200.
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  - Schumacher, Maria A., Elham Karamooz, Alena Zíková, Lukás Trantírek, and Julius Lukes. “Crystal structures of T. brucei MRP1/MRP2 guide-RNA binding complex reveal RNA matchmaking mechanism.” Cell 126, no. 4 (August 25, 2006): 701–11. https://doi.org/10.1016/j.cell.2006.06.047.
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  - Schumacher, Maria A., Gerald Seidel, Wolfgang Hillen, and Richard G. Brennan. “Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation.” J Biol Chem 281, no. 10 (March 10, 2006): 6793–6800. https://doi.org/10.1074/jbc.M509977200.
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  - Schumacher, Maria A., and Barbara E. Funnell. “Structures of ParB bound to DNA reveal mechanism of partition complex formation.” Nature 438, no. 7067 (November 24, 2005): 516–19. https://doi.org/10.1038/nature04149.
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  - Schumacher, Maria, Kazunori Mizuno, and Hans Peter Bächinger. “The crystal structure of the collagen-like polypeptide (glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)9 at 1.55 A resolution shows up-puckering of the proline ring in the Xaa position.” J Biol Chem 280, no. 21 (May 27, 2005): 20397–403. https://doi.org/10.1074/jbc.M501453200.
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  - Schumacher, Maria A., Gregory S. Allen, Marco Diel, Gerald Seidel, Wolfgang Hillen, and Richard G. Brennan. “Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P.” Cell 118, no. 6 (September 17, 2004): 731–41. https://doi.org/10.1016/j.cell.2004.08.027.
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  - Schumacher, Maria A., Marshall C. Miller, and Richard G. Brennan. “Structural mechanism of the simultaneous binding of two drugs to a multidrug-binding protein.” The Embo Journal 23, no. 15 (August 2004): 2923–30. https://doi.org/10.1038/sj.emboj.7600288.
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  - Schumacher, Maria A., Matthew Crum, and Marshall C. Miller. “Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex.” Structure 12, no. 5 (May 2004): 849–60. https://doi.org/10.1016/j.str.2004.03.017.
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  - Murray, David S., Maria A. Schumacher, and Richard G. Brennan. “Crystal structures of QacR-diamidine complexes reveal additional multidrug-binding modes and a novel mechanism of drug charge neutralization.” J Biol Chem 279, no. 14 (April 2, 2004): 14365–71. https://doi.org/10.1074/jbc.M313870200.
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  - Schumacher, Maria A., Audrey O. T. Lau, and Patricia J. Johnson. “Structural basis of core promoter recognition in a primitive eukaryote.” Cell 115, no. 4 (November 14, 2003): 413–24. https://doi.org/10.1016/s0092-8674(03)00887-0.
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  - Schumacher, Maria A., and Richard G. Brennan. “Deciphering the molecular basis of multidrug recognition: crystal structures of the Staphylococcus aureus multidrug binding transcription regulator QacR.” Res Microbiol 154, no. 2 (March 2003): 69–77. https://doi.org/10.1016/S0923-2508(02)00013-X.
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  - Bruening-Wright, Andrew, Maria A. Schumacher, John P. Adelman, and James Maylie. “Localization of the activation gate for small conductance Ca2+-activated K+ channels.” J Neurosci 22, no. 15 (August 1, 2002): 6499–6506.
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  - Schumacher, Maria A., and Richard G. Brennan. “Structural mechanisms of multidrug recognition and regulation by bacterial multidrug transcription factors.” Mol Microbiol 45, no. 4 (August 2002): 885–93. https://doi.org/10.1046/j.1365-2958.2002.03039.x.
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  - Schumacher, Maria A., Robert F. Pearson, Thorleif Møller, Poul Valentin-Hansen, and Richard G. Brennan. “Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein.” Embo J 21, no. 13 (July 1, 2002): 3546–56. https://doi.org/10.1093/emboj/cdf322.
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  - Schumacher, Maria, and John P. Adelman. “Ion channels: an open and shut case.” Nature 417, no. 6888 (May 30, 2002): 501–2. https://doi.org/10.1038/417501a.
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  - Schumacher, M. A., M. C. Miller, S. Grkovic, M. H. Brown, R. A. Skurray, and R. G. Brennan. “Erratum: Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR (EMBO Journal (2002) 21 (1210-1218)).” Embo Journal 21, no. 9 (May 1, 2002): 2301. https://doi.org/10.1093/emboj/21.9.2301.
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  - Schumacher, Maria A., Jacob L. Todd, Adrian E. Rice, Kirk G. Tanner, and John M. Denu. “Structural basis for the recognition of a bisphosphorylated MAP kinase peptide by human VHR protein Phosphatase.” Biochemistry 41, no. 9 (March 2002): 3009–17. https://doi.org/10.1021/bi015799l.
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  - Schumacher, Maria A., Marshall C. Miller, Steve Grkovic, Melissa H. Brown, Ronald A. Skurray, and Richard G. Brennan. “Structural basis for cooperative DNA binding by two dimers of the multidrug-binding protein QacR.” Embo J 21, no. 5 (March 1, 2002): 1210–18. https://doi.org/10.1093/emboj/21.5.1210.
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  - Schumacher, Maria A., Caleb J. Bashor, Minsun Hong Song, Kanao Otsu, Shuren Zhu, Ronald J. Parry, Buddy Ullman, and Richard G. Brennan. “The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase.” Proc Natl Acad Sci U S A 99, no. 1 (January 8, 2002): 78–83. https://doi.org/10.1073/pnas.012399599.
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  - Schumacher, M. A., M. C. Miller, S. Grkovic, M. H. Brown, R. A. Skurray, and R. G. Brennan. “Structural mechanisms of QacR induction and multidrug recognition.” Science 294, no. 5549 (December 7, 2001): 2158–63. https://doi.org/10.1126/science.1066020.
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  - Grkovic, S., M. H. Brown, M. A. Schumacher, R. G. Brennan, and R. A. Skurray. “The staphylococcal QacR multidrug regulator binds a correctly spaced operator as a pair of dimers.” J Bacteriol 183, no. 24 (December 2001): 7102–9. https://doi.org/10.1128/JB.183.24.7102-7109.2001.
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  - Schumacher, M. A., B. K. Hurlburt, and R. G. Brennan. “Erratum: Crystal structures of SarA, a pleiotropic regulator of virulence genes in S. aureus (Nature (20010 409 (215-219)).” Nature 414, no. 6859 (November 1, 2001): 85. https://doi.org/10.1038/35102089.
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  - Schumacher, M. A., A. F. Rivard, H. P. Bächinger, and J. P. Adelman. “Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin.” Nature 410, no. 6832 (April 26, 2001): 1120–24. https://doi.org/10.1038/35074145.
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  - Craig, J. C., M. A. Schumacher, S. E. Mansoor, D. L. Farrens, R. G. Brennan, and R. H. Goodman. “Consensus and variant cAMP-regulated enhancers have distinct CREB-binding properties.” J Biol Chem 276, no. 15 (April 13, 2001): 11719–28. https://doi.org/10.1074/jbc.M010263200.
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  - Schumacher, M. A., B. K. Hurlburt, and R. G. Brennan. “Crystal structures of SarA, a pleiotropic regulator of virulence genes in S. aureus.” Nature 409, no. 6817 (January 11, 2001): 215–19. https://doi.org/10.1038/35051623.
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  - Schumacher, M. A., R. H. Goodman, and R. G. Brennan. “The structure of a CREB bZIP.somatostatin CRE complex reveals the basis for selective dimerization and divalent cation-enhanced DNA binding.” J Biol Chem 275, no. 45 (November 10, 2000): 35242–47. https://doi.org/10.1074/jbc.M007293200.
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  - Brown, M., M. A. Schumacher, G. D. Wiens, R. G. Brennan, and M. B. Rittenberg. “The structural basis of repertoire shift in an immune response to phosphocholine.” J Exp Med 191, no. 12 (June 19, 2000): 2101–12. https://doi.org/10.1084/jem.191.12.2101.
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  - Schumacher, M. A., D. M. Scott, I. I. Mathews, S. E. Ealick, D. S. Roos, B. Ullman, and R. G. Brennan. “Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.” J Mol Biol 298, no. 5 (May 19, 2000): 875–93. https://doi.org/10.1006/jmbi.2000.3753.
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  - Schumacher, M. A., D. M. Scott, I. I. Mathews, S. E. Ealick, D. S. Roos, B. Ullman, and R. G. Brennan. “Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.” J Mol Biol 296, no. 2 (February 18, 2000): 549–67. https://doi.org/10.1006/jmbi.1999.3474.
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  - Glasfeld, A., A. N. Koehler, M. A. Schumacher, and R. G. Brennan. “The role of lysine 55 in determining the specificity of the purine repressor for its operators through minor groove interactions.” Journal of Molecular Biology 291, no. 2 (August 1999): 347–61. https://doi.org/10.1006/jmbi.1999.2946.
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  - Rechtin, T. M., A. F. Gillaspy, M. A. Schumacher, R. G. Brennan, M. S. Smeltzer, and B. K. Hurlburt. “Characterization of the SarA virulence gene regulator of Staphylococcus aureus.” Mol Microbiol 33, no. 2 (July 1999): 307–16. https://doi.org/10.1046/j.1365-2958.1999.01474.x.
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  - Schumacher, M. A., D. Carter, D. M. Scott, D. S. Roos, B. Ullman, and R. G. Brennan. “Crystal structures of Toxoplasma gondii uracil phosphoribosyltransferase reveal the atomic basis of pyrimidine discrimination and prodrug binding.” The Embo Journal 17, no. 12 (June 1998): 3219–32. https://doi.org/10.1093/emboj/17.12.3219.
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  - Lu, F., M. A. Schumacher, D. N. Arvidson, A. Haldimann, B. L. Wanner, H. Zalkin, and R. G. Brennan. “Structure-based redesign of corepressor specificity of the Escherichia coli purine repressor by substitution of residue 190.” Biochemistry 37, no. 4 (January 1998): 971–82. https://doi.org/10.1021/bi971942s.
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  - Schumacher, M. A., A. Glasfeld, H. Zalkin, and R. G. Brennan. “The X-ray structure of the PurR-guanine-purF operator complex reveals the contributions of complementary electrostatic surfaces and a water-mediated hydrogen bond to corepressor specificity and binding affinity.” J Biol Chem 272, no. 36 (September 5, 1997): 22648–53. https://doi.org/10.1074/jbc.272.36.22648.
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  - Schumacher, M. A., E. E. Zheleznova, K. S. Poundstone, R. Kluger, R. T. Jones, and R. G. Brennan. “Allosteric intermediates indicate R2 is the liganded hemoglobin end state.” Proc Natl Acad Sci U S A 94, no. 15 (July 22, 1997): 7841–44. https://doi.org/10.1073/pnas.94.15.7841.
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  - Glasfeld, A., M. A. Schumacher, K. Y. Choi, H. Zalkin, and R. G. Brennan. “A positively charged residue bound in the minor groove does not alter the bending of a DNA duplex.” Journal of the American Chemical Society 118, no. 51 (December 25, 1996): 13073–74. https://doi.org/10.1021/ja962416b.
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  - Schumacher, M. A., D. Carter, D. S. Roos, B. Ullman, and R. G. Brennan. “Crystal structures of Toxoplasma gondii HGXPRTase reveal the catalytic role of a long flexible loop.” Nat Struct Biol 3, no. 10 (October 1996): 881–87. https://doi.org/10.1038/nsb1096-881.
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  - Lewis, M., G. Chang, N. C. Horton, M. A. Kercher, H. C. Pace, M. A. Schumacher, R. G. Brennan, and P. Lu. “Crystal structure of the lactose operon repressor and its complexes with DNA and inducer.” Science 271, no. 5253 (March 1, 1996): 1247–54. https://doi.org/10.1126/science.271.5253.1247.
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  - Nagadoi, A., S. Morikawa, H. Nakamura, M. Enari, K. Kobayashi, H. Yamamoto, G. Sampei, K. Mizobuchi, M. A. Schumacher, and R. G. Brennan. “Structural comparison of the free and DNA-bound forms of the purine repressor DNA-binding domain.” Structure (London, England : 1993) 3, no. 11 (November 1995): 1217–24. https://doi.org/10.1016/s0969-2126(01)00257-x.
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  - Schumacher, M. A., K. Y. Choi, F. Lu, H. Zalkin, and R. G. Brennan. “Mechanism of corepressor-mediated specific DNA binding by the purine repressor.” Cell 83, no. 1 (October 6, 1995): 147–55. https://doi.org/10.1016/0092-8674(95)90243-0.
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  - Schumacher, M. A., M. M. Dixon, R. Kluger, R. T. Jones, and R. G. Brennan. “Allosteric transition intermediates modelled by crosslinked haemoglobins.” Nature 375, no. 6526 (May 1995): 84–87. https://doi.org/10.1038/375084a0.
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  - Nagadoi, A., K. Nakazawa, S. Morikawa, H. Nakamura, G. Sampei, K. Mizobuchi, H. Yamamoto, M. A. Schumacher, R. G. Brennan, and Y. Nishimura. “Conformational changes of purine repressor DNA-binding domain upon complexation with DNA.” Nucleic Acids Symp Ser, no. 34 (1995): 63–64.
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  - Schumacher, M. A., K. Y. Choi, H. Zalkin, and R. G. Brennan. “Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices.” Science (New York, N.Y.) 266, no. 5186 (November 1994): 763–70. https://doi.org/10.1126/science.7973627.
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  - Schumacher, M. A., K. Y. Choi, H. Zalkin, and R. G. Brennan. “Crystallization and preliminary X-ray analysis of an Escherichia coli purine repressor-hypoxanthine-DNA complex.” Journal of Molecular Biology 242, no. 3 (September 1994): 302–5. https://doi.org/10.1006/jmbi.1994.1580.
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  - Schumacher, M. A., J. R. Macdonald, J. Björkman, S. L. Mowbray, and R. G. Brennan. “Structural analysis of the purine repressor, an Escherichia coli DNA-binding protein.” J Biol Chem 268, no. 17 (June 15, 1993): 12282–88.
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  - Schumacher, M. A., K. Y. Choi, H. Zalkin, and R. G. Brennan. “Crystallization and preliminary X-ray studies on the co-repressor binding domain of the Escherichia coli purine repressor.” J Mol Biol 225, no. 4 (June 20, 1992): 1131–33. https://doi.org/10.1016/0022-2836(92)90111-v.
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