Arno Lee Greenleaf | Scholars@Duke

Arno Lee Greenleaf
Professor of Biochemistry

My laboratory studies the mechanisms by which different activities in the cell nucleus are connected to the transcription machinery via interactions with the hyper-phosphorylated C-terminal repeat domain (PCTD) of elongating RNA polymerase II. Differential phosphorylation of the CTD, as the RNAP proceeds through successive stages of transcription, orchestrates sequential recruitment of factors to the transcriptase; this serves to coordinate RNA processing events and mRNA nuclear export with gene transcription. To gain a thorough understanding of relevant phosphorylation events on the PCTD, we identified the principal elongation-phase CTD kinase activities in three different eukaryotes, yeast (yCtk1), Drosophila (dCDK12) and humans (hCDK12 & 13). In addition, we described a novel set of phosphoCTD-associating proteins (“PCAPs”) that we now are investigating primarily in human cells. Our results revealed novel roles for elongating RNAPII, and they engendered several totally new lines of investigation.

Recently hCDK12 was shown to be a tumor suppressor for ovarian cancer, and our investigations of this kinase will illuminate its features that, when mutated, can lead to ovarian cancer.

In another cancer-related project, we are identifying drug targets for a new class of drugs to be aimed at ovarian and breast cancers.

Current Appointments & Affiliations

Professor of Biochemistry, Biochemistry, Basic Science Departments 1990
Member of the Duke Cancer Institute, Duke Cancer Institute, Institutes and Centers 1977

Contact Information

0034 CARL Building, Duke Box 3711, Durham, NC 27710
Duke Box 3711, Durham, NC 27710
arno@duke.edu (919) 684-4034

Background
Education, Training, & Certifications
- Ph.D., Harvard University 1974
Duke Appointment History
- Professor in Molecular Genetics and Microbiology, Molecular Genetics and Microbiology, Basic Science Departments 2010 - 2019
- Assistant Professor of Biochemistry, Biochemistry, Basic Science Departments 1977 - 1990
Recognition
Awards & Honors
- Elected Fellow of AAAS. American Association for the Advancement of Science, The. 2012
Research
Selected Grants
- Organization and Function of Cellular Structure awarded by National Institutes of Health 1975 - 2020
- TUMOR-SELECTIVE DRUGS TARGETING BREAST & OVARIAN CANCER awarded by North Carolina Biotechnology Center 2017 - 2019
- Phosphorylation and Functions of the RNA Polymerase CTD awarded by National Institutes of Health 1988 - 2016
- Connections between mRNA elongation and splicing awarded by National Institutes of Health 2004 - 2009
- Role of PhosphoCTD in Spliceosome Assembly awarded by National Science Foundation 2001 - 2004
- Ctd Kinase And Transcription Dynamics awarded by National Institutes of Health 1996 - 1999
- Ctd Kinase And Rna Polymerase Ii Phosphorylation awarded by National Institutes of Health 1988 - 1999
- Transcriptase Kinase From Yeast And Drosophila awarded by National Institutes of Health 1988 - 1996
- Rna Polymerase Ii Subunits And Transcription Factors awarded by National Institutes of Health 1990 - 1996
- Transcriptase Kinases From Yeast And Drosophila awarded by National Institutes of Health 1993 - 1995
- Transcriptase Kinase From Drosophila And Yeast awarded by National Institutes of Health 1990 - 1991
- Transcriptase Kinase From Droxophila And Yeast awarded by National Institutes of Health 1989 - 1991
- Biochemical Genetics Of Drosophila Rna Polymerase Ii awarded by National Institutes of Health 1989 - 1990
External Relationships
- INCA Therapeutics Corporation.
Publications & Artistic Works
Selected Publications
- Academic Articles
  - Bartkowiak, Bartlomiej, Christopher M. Yan, Erik J. Soderblom, and Arno L. Greenleaf. “CDK12 Activity-Dependent Phosphorylation Events in Human Cells.” Biomolecules 9, no. 10 (October 22, 2019). https://doi.org/10.3390/biom9100634.
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  - Greenleaf, Arno L. “Human CDK12 and CDK13, multi-tasking CTD kinases for the new millenium.” Transcription 10, no. 2 (April 2019): 91–110. https://doi.org/10.1080/21541264.2018.1535211.
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  - Zhang, Tinghu, Nicholas Kwiatkowski, Calla M. Olson, Sarah E. Dixon-Clarke, Brian J. Abraham, Ann K. Greifenberg, Scott B. Ficarro, et al. “Covalent targeting of remote cysteine residues to develop CDK12 and CDK13 inhibitors.” Nat Chem Biol 12, no. 10 (October 2016): 876–84. https://doi.org/10.1038/nchembio.2166.
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  - Bartkowiak, Bartlomiej, Christopher Yan, and Arno L. Greenleaf. “Engineering an analog-sensitive CDK12 cell line using CRISPR/Cas.” Biochim Biophys Acta 1849, no. 9 (September 2015): 1179–87. https://doi.org/10.1016/j.bbagrm.2015.07.010.
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  - Bartkowiak, Bartlomiej, and Arno L. Greenleaf. “Expression, purification, and identification of associated proteins of the full-length hCDK12/CyclinK complex.” J Biol Chem 290, no. 3 (January 16, 2015): 1786–95. https://doi.org/10.1074/jbc.M114.612226.
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  - Liu, Jiangxin, Shilong Fan, Chul-Jin Lee, Arno L. Greenleaf, and Pei Zhou. “Specific interaction of the transcription elongation regulator TCERG1 with RNA polymerase II requires simultaneous phosphorylation at Ser2, Ser5, and Ser7 within the carboxyl-terminal domain repeat.” J Biol Chem 288, no. 15 (April 12, 2013): 10890–901. https://doi.org/10.1074/jbc.M113.460238.
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  - Winsor, Tiffany Sabin, Bartlomiej Bartkowiak, Craig B. Bennett, and Arno L. Greenleaf. “A DNA damage response system associated with the phosphoCTD of elongating RNA polymerase II.” Plos One 8, no. 4 (2013): e60909. https://doi.org/10.1371/journal.pone.0060909.
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  - Möller, André, Sheila Q. Xie, Fabian Hosp, Benjamin Lang, Hemali P. Phatnani, Sonya James, Francisco Ramirez, et al. “Proteomic analysis of mitotic RNA polymerase II reveals novel interactors and association with proteins dysfunctional in disease.” Mol Cell Proteomics 11, no. 6 (June 2012): M111.011767. https://doi.org/10.1074/mcp.M111.011767.
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  - MacKellar, April L., and Arno L. Greenleaf. “Cotranscriptional association of mRNA export factor Yra1 with C-terminal domain of RNA polymerase II.” J Biol Chem 286, no. 42 (October 21, 2011): 36385–95. https://doi.org/10.1074/jbc.M111.268144.
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  - Bartkowiak, Bartlomiej, and Arno L. Greenleaf. “Phosphorylation of RNAPII: To P-TEFb or not to P-TEFb?” Transcription 2, no. 3 (May 2011): 115–19. https://doi.org/10.4161/trns.2.3.15004.
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  - Werner-Allen, Jon W., Chul-Jin Lee, Pengda Liu, Nathan I. Nicely, Su Wang, Arno L. Greenleaf, and Pei Zhou. “cis-Proline-mediated Ser(P)5 dephosphorylation by the RNA polymerase II C-terminal domain phosphatase Ssu72.” J Biol Chem 286, no. 7 (February 18, 2011): 5717–26. https://doi.org/10.1074/jbc.M110.197129.
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  - Bartkowiak, Bartlomiej, April L. Mackellar, and Arno L. Greenleaf. “Updating the CTD Story: From Tail to Epic.” Genet Res Int 2011 (2011): 623718. https://doi.org/10.4061/2011/623718.
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  - Kanagaraj, Radhakrishnan, Daniela Huehn, April MacKellar, Mirco Menigatti, Lu Zheng, Vaclav Urban, Igor Shevelev, Arno L. Greenleaf, and Pavel Janscak. “RECQ5 helicase associates with the C-terminal repeat domain of RNA polymerase II during productive elongation phase of transcription.” Nucleic Acids Res 38, no. 22 (December 2010): 8131–40. https://doi.org/10.1093/nar/gkq697.
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  - Liu, Pengda, John M. Kenney, John W. Stiller, and Arno L. Greenleaf. “Genetic organization, length conservation, and evolution of RNA polymerase II carboxyl-terminal domain.” Mol Biol Evol 27, no. 11 (November 2010): 2628–41. https://doi.org/10.1093/molbev/msq151.
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  - Bartkowiak, Bartlomiej, Pengda Liu, Hemali P. Phatnani, Nicholas J. Fuda, Jeffrey J. Cooper, David H. Price, Karen Adelman, John T. Lis, and Arno L. Greenleaf. “CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1.” Genes Dev 24, no. 20 (October 15, 2010): 2303–16. https://doi.org/10.1101/gad.1968210.
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  - Wu, Jianhong, Hemali P. Phatnani, Tao-Shih Hsieh, and Arno L. Greenleaf. “The phosphoCTD-interacting domain of Topoisomerase I.” Biochem Biophys Res Commun 397, no. 1 (June 18, 2010): 117–19. https://doi.org/10.1016/j.bbrc.2010.05.081.
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  - Westmoreland, Tammy J., Sajith M. Wickramasekara, Andrew Y. Guo, Alice L. Selim, Tiffany S. Winsor, Arno L. Greenleaf, Kimberly L. Blackwell, John A. Olson, Jeffrey R. Marks, and Craig B. Bennett. “Comparative genome-wide screening identifies a conserved doxorubicin repair network that is diploid specific in Saccharomyces cerevisiae.” Plos One 4, no. 6 (June 8, 2009): e5830. https://doi.org/10.1371/journal.pone.0005830.
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  - MacKellar, April L., and Arno L. Greenleaf. “Association of mRNA Export Factor Yra1 with the C-terminal Domain of RNA Polymerase II.” Faseb Journal 23 (April 1, 2009).
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  - Liu, Pengda, Arno L. Greenleaf, and John W. Stiller. “The essential sequence elements required for RNAP II carboxyl-terminal domain function in yeast and their evolutionary conservation.” Mol Biol Evol 25, no. 4 (April 2008): 719–27. https://doi.org/10.1093/molbev/msn017.
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  - Bennett, Craig B., Tammy J. Westmoreland, Carmel S. Verrier, Carrie A. B. Blanchette, Tiffany L. Sabin, Hemali P. Phatnani, Yuliya V. Mishina, et al. “Yeast screens identify the RNA polymerase II CTD and SPT5 as relevant targets of BRCA1 interaction.” Plos One 3, no. 1 (January 16, 2008): e1448. https://doi.org/10.1371/journal.pone.0001448.
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  - Phatnani, Hemali P., and Arno L. Greenleaf. “Phosphorylation and functions of the RNA polymerase II CTD.” Genes Dev 20, no. 21 (November 1, 2006): 2922–36. https://doi.org/10.1101/gad.1477006.
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  - Li, Ming, Hemali P. Phatnani, Arno L. Greenleaf, and Pei Zhou. “NMR assignment of the SRI domain of human Set2/HYPB.” J Biomol Nmr 36 Suppl 1 (2006): 5. https://doi.org/10.1007/s10858-005-4690-8.
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  - Li, Ming, Hemali P. Phatnani, Ziqiang Guan, Harvey Sage, Arno L. Greenleaf, and Pei Zhou. “Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1.” Proc Natl Acad Sci U S A 102, no. 49 (December 6, 2005): 17636–41. https://doi.org/10.1073/pnas.0506350102.
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  - Kizer, Kelby O., Hemali P. Phatnani, Yoichiro Shibata, Hana Hall, Arno L. Greenleaf, and Brian D. Strahl. “A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation.” Mol Cell Biol 25, no. 8 (April 2005): 3305–16. https://doi.org/10.1128/MCB.25.8.3305-3316.2005.
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  - Phatnani, Hemali P., Janice C. Jones, and Arno L. Greenleaf. “Expanding the functional repertoire of CTD kinase I and RNA polymerase II: novel phosphoCTD-associating proteins in the yeast proteome.” Biochemistry 43, no. 50 (December 21, 2004): 15702–19. https://doi.org/10.1021/bi048364h.
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  - Jones, Janice C., Hemali P. Phatnani, Timothy A. Haystead, Justin A. MacDonald, S Munir Alam, and Arno L. Greenleaf. “C-terminal repeat domain kinase I phosphorylates Ser2 and Ser5 of RNA polymerase II C-terminal domain repeats.” J Biol Chem 279, no. 24 (June 11, 2004): 24957–64. https://doi.org/10.1074/jbc.M402218200.
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  - Phatnani, Hemali P., and Arno L. Greenleaf. “Identifying phosphoCTD-associating proteins.” Methods Mol Biol 257 (2004): 17–28. https://doi.org/10.1385/1-59259-750-5:017.
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  - Greenleaf, Arno. “Getting a grip on the CTD of Pol II.” Structure 11, no. 8 (August 2003): 900–902. https://doi.org/10.1016/s0969-2126(03)00164-3.
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  - Skaar, David A., and Arno L. Greenleaf. “The RNA polymerase II CTD kinase CTDK-I affects pre-mRNA 3' cleavage/polyadenylation through the processing component Pti1p.” Mol Cell 10, no. 6 (December 2002): 1429–39. https://doi.org/10.1016/s1097-2765(02)00731-1.
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  - Carty, Sherry M., and Arno L. Greenleaf. “Hyperphosphorylated C-terminal repeat domain-associating proteins in the nuclear proteome link transcription to DNA/chromatin modification and RNA processing.” Mol Cell Proteomics 1, no. 8 (August 2002): 598–610. https://doi.org/10.1074/mcp.m200029-mcp200.
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  - Goldstrohm, A. C., A. L. Greenleaf, and M. A. Garcia-Blanco. “Co-transcriptional splicing of pre-messenger RNAs: considerations for the mechanism of alternative splicing.” Gene 277, no. 1–2 (October 17, 2001): 31–47. https://doi.org/10.1016/s0378-1119(01)00695-3.
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  - Myers, J. K., D. P. Morris, A. L. Greenleaf, and T. G. Oas. “Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1.” Biochemistry 40, no. 29 (July 24, 2001): 8479–86. https://doi.org/10.1021/bi0027884.
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  - Chao, S. H., A. L. Greenleaf, and D. H. Price. “Juglone, an inhibitor of the peptidyl-prolyl isomerase Pin1, also directly blocks transcription.” Nucleic Acids Res 29, no. 3 (February 1, 2001): 767–73. https://doi.org/10.1093/nar/29.3.767.
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  - Morris, D. P., and A. L. Greenleaf. “The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II.” J Biol Chem 275, no. 51 (December 22, 2000): 39935–43. https://doi.org/10.1074/jbc.M004118200.
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  - Carty, S. M., A. C. Goldstrohm, C. Suñé, M. A. Garcia-Blanco, and A. L. Greenleaf. “Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II.” Proc Natl Acad Sci U S A 97, no. 16 (August 1, 2000): 9015–20. https://doi.org/10.1073/pnas.160266597.
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  - Carty, S. M., M. Wilborn, and A. L. Greenleaf. “Novel interactions with the phospho-CTD of RNA polymerase II: Connecting transcription with DNA remodeling.” Faseb Journal 14, no. 8 (May 11, 2000): A1582–A1582.
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  - Rodriguez, C. R., E. J. Cho, M. C. Keogh, C. L. Moore, A. L. Greenleaf, and S. Buratowski. “Kin28, the TFIIH-associated carboxy-terminal domain kinase, facilitates the recruitment of mRNA processing machinery to RNA polymerase II.” Mol Cell Biol 20, no. 1 (January 2000): 104–12. https://doi.org/10.1128/mcb.20.1.104-112.2000.
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  - Morris, D. P., H. P. Phatnani, and A. L. Greenleaf. “Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3'-End formation.” J Biol Chem 274, no. 44 (October 29, 1999): 31583–87. https://doi.org/10.1074/jbc.274.44.31583.
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  - Egyházi, E., A. Ossoinak, J. M. Lee, A. L. Greenleaf, T. P. Mäkelä, and A. Pigon. “Heat-shock-specific phosphorylation and transcriptional activity of RNA polymerase II.” Exp Cell Res 242, no. 1 (July 10, 1998): 211–21. https://doi.org/10.1006/excr.1998.4112.
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  - Morris, D. P., R. D. Stevens, and A. L. Greenleaf. “Protonation of the neutral repeats of the RNA polymerase II CTD.” Biochem Biophys Res Commun 245, no. 1 (April 7, 1998): 53–58. https://doi.org/10.1006/bbrc.1998.8373.
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  - Morris, D. P., J. M. Lee, D. E. Sterner, W. J. Brickey, and A. L. Greenleaf. “Assaying CTD kinases in vitro and phosphorylation-modulated properties of RNA polymerase II in vivo.” Methods 12, no. 3 (July 1997): 264–75. https://doi.org/10.1006/meth.1997.0478.
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  - Lee, J. M., and A. L. Greenleaf. “Modulation of RNA polymerase II elongation efficiency by C-terminal heptapeptide repeat domain kinase I.” J Biol Chem 272, no. 17 (April 25, 1997): 10990–93. https://doi.org/10.1074/jbc.272.17.10990.
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  - Li, B., J. A. Weber, Y. Chen, A. L. Greenleaf, and D. S. Gilmour. “Analyses of promoter-proximal pausing by RNA polymerase II on the hsp70 heat shock gene promoter in a Drosophila nuclear extract.” Mol Cell Biol 16, no. 10 (October 1996): 5433–43. https://doi.org/10.1128/mcb.16.10.5433.
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  - Chen, Y., D. Chafin, D. H. Price, and A. L. Greenleaf. “Drosophila RNA polymerase II mutants that affect transcription elongation.” J Biol Chem 271, no. 11 (March 15, 1996): 5993–99.
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  - Egyházi, E., A. Ossoinak, A. Pigon, C. Holmgren, J. M. Lee, and A. L. Greenleaf. “Phosphorylation dependence of the initiation of productive transcription of Balbiani ring 2 genes in living cells.” Chromosoma 104, no. 6 (March 1996): 422–33. https://doi.org/10.1007/BF00352266.
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  - EGYHAZI, E., A. OSSOINAK, A. PIGON, J. M. LEE, and A. L. GREENLEAF. “DIFFERENTIAL INHIBITORY EFFECT OF DRB ON THE TRANSCRIPTIONAL ACTIVITY AND PHOSPHORYLATION OF RNA-POLYMERASE-II IN HEAT-SHOCKED AND NONSHOCKED CELLS.” Molecular Biology of the Cell 6 (November 1, 1995): 439–439.
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  - Sterner, D. E., J. M. Lee, S. E. Hardin, and A. L. Greenleaf. “The yeast carboxyl-terminal repeat domain kinase CTDK-I is a divergent cyclin-cyclin-dependent kinase complex.” Mol Cell Biol 15, no. 10 (October 1995): 5716–24. https://doi.org/10.1128/mcb.15.10.5716.
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  - Brickey, W. J., and A. L. Greenleaf. “Functional studies of the carboxy-terminal repeat domain of Drosophila RNA polymerase II in vivo.” Genetics 140, no. 2 (June 1995): 599–613.
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  - Skantar, A. M., and A. L. Greenleaf. “Identifying a transcription factor interaction site on RNA polymerase II.” Gene Expr 5, no. 1 (1995): 49–69.
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  - O’Brien, T., S. Hardin, A. Greenleaf, and J. T. Lis. “Phosphorylation of RNA polymerase II C-terminal domain and transcriptional elongation.” Nature 370, no. 6484 (July 7, 1994): 75–77. https://doi.org/10.1038/370075a0.
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  - WEEKS, J. R., S. HARDIN, J. J. SHEN, J. M. LEE, and A. L. GREENLEAF. “RNA-POLYMERASE-II CTD PHOSPHORYLATION IN-VIVO.” Journal of Cellular Biochemistry, February 13, 1994, 3–3.
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  - Greenleaf, A. L. “A positive addition to a negative tail's tale.” Proc Natl Acad Sci U S A 90, no. 23 (December 1, 1993): 10896–97. https://doi.org/10.1073/pnas.90.23.10896.
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  - Weeks, J. R., S. E. Hardin, J. Shen, J. M. Lee, and A. L. Greenleaf. “Locus-specific variation in phosphorylation state of RNA polymerase II in vivo: correlations with gene activity and transcript processing.” Genes Dev 7, no. 12A (December 1993): 2329–44. https://doi.org/10.1101/gad.7.12a.2329.
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  - Chen, Y., J. Weeks, M. A. Mortin, and A. L. Greenleaf. “Mapping mutations in genes encoding the two large subunits of Drosophila RNA polymerase II defines domains essential for basic transcription functions and for proper expression of developmental genes.” Mol Cell Biol 13, no. 7 (July 1993): 4214–22. https://doi.org/10.1128/mcb.13.7.4214.
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  - Hamilton, B. J., M. A. Mortin, and A. L. Greenleaf. “Reverse genetics of Drosophila RNA polymerase II: identification and characterization of RpII140, the genomic locus for the second-largest subunit.” Genetics 134, no. 2 (June 1993): 517–29.
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  - Greenleaf, A. L. “Positive patches and negative noodles: linking RNA processing to transcription?” Trends Biochem Sci 18, no. 4 (April 1993): 117–19. https://doi.org/10.1016/0968-0004(93)90016-g.
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  - Lee, J. M., and A. L. Greenleaf. “CTD kinase large subunit is encoded by CTK1, a gene required for normal growth of Saccharomyces cerevisiae.” Gene Expr 1, no. 2 (May 1991): 149–67.
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  - Zehring, W. A., and A. L. Greenleaf. “The carboxyl-terminal repeat domain of RNA polymerase II is not required for transcription factor Sp1 to function in vitro.” J Biol Chem 265, no. 15 (May 25, 1990): 8351–53.
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  - Sluder, A. E., A. L. Greenleaf, and D. H. Price. “Properties of a Drosophila RNA polymerase II elongation factor.” J Biol Chem 264, no. 15 (May 25, 1989): 8963–69.
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  - Lee, J. M., and A. L. Greenleaf. “A protein kinase that phosphorylates the C-terminal repeat domain of the largest subunit of RNA polymerase II.” Proc Natl Acad Sci U S A 86, no. 10 (May 1989): 3624–28. https://doi.org/10.1073/pnas.86.10.3624.
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  - Price, D. H., A. E. Sluder, and A. L. Greenleaf. “Dynamic interaction between a Drosophila transcription factor and RNA polymerase II.” Mol Cell Biol 9, no. 4 (April 1989): 1465–75. https://doi.org/10.1128/mcb.9.4.1465.
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  - Fisher, P. A., L. Lin, M. McConnell, A. Greenleaf, J. M. Lee, and D. E. Smith. “Heat shock-induced appearance of RNA polymerase II in karyoskeletal protein-enriched (nuclear "matrix") fractions correlates with transcriptional shutdown in Drosophila melanogaster.” J Biol Chem 264, no. 6 (February 25, 1989): 3464–69.
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  - Jokerst, R. S., J. R. Weeks, W. A. Zehring, and A. L. Greenleaf. “Analysis of the gene encoding the largest subunit of RNA polymerase II in Drosophila.” Mol Gen Genet 215, no. 2 (January 1989): 266–75. https://doi.org/10.1007/BF00339727.
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  - Sluder, A. E., D. H. Price, and A. L. Greenleaf. “Elongation by Drosophila RNA polymerase II. Transcription of 3'-extended DNA templates.” J Biol Chem 263, no. 20 (July 15, 1988): 9917–25.
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  - Zehring, W. A., J. M. Lee, J. R. Weeks, R. S. Jokerst, and A. L. Greenleaf. “The C-terminal repeat domain of RNA polymerase II largest subunit is essential in vivo but is not required for accurate transcription initiation in vitro.” Proc Natl Acad Sci U S A 85, no. 11 (June 1988): 3698–3702. https://doi.org/10.1073/pnas.85.11.3698.
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  - Sluder, A. E., D. H. Price, and A. L. Greenleaf. “An activity necessary for in vitro transcription is a DNase inhibitor.” Biochimie 69, no. 11–12 (November 1987): 1199–1205. https://doi.org/10.1016/0300-9084(87)90147-7.
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  - Price, D. H., A. E. Sluder, and A. L. Greenleaf. “Fractionation of transcription factors for RNA polymerase II from Drosophila Kc cell nuclear extracts.” J Biol Chem 262, no. 7 (March 5, 1987): 3244–55.
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  - Searles, L. L., A. L. Greenleaf, W. E. Kemp, and R. A. Voelker. “Sites of P element insertion and structures of P element deletions in the 5' region of Drosophila melanogaster RpII215.” Mol Cell Biol 6, no. 10 (October 1986): 3312–19. https://doi.org/10.1128/mcb.6.10.3312.
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  - Kelly, J. L., A. L. Greenleaf, and I. R. Lehman. “Isolation of the nuclear gene encoding a subunit of the yeast mitochondrial RNA polymerase.” J Biol Chem 261, no. 22 (August 5, 1986): 10348–51.
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  - Greenleaf, A. L., J. L. Kelly, and I. R. Lehman. “Yeast RPO41 gene product is required for transcription and maintenance of the mitochondrial genome.” Proc Natl Acad Sci U S A 83, no. 10 (May 1986): 3391–94. https://doi.org/10.1073/pnas.83.10.3391.
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  - Skripal, I. G., J. R. Weeks, and A. L. Greenleaf. “Dye-ligand affinity chromatography of RNA polymerase II.” Acta Biochim Biophys Hung 21, no. 3 (1986): 215–24.
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  - Coulter, D. E., and A. L. Greenleaf. “A mutation in the largest subunit of RNA polymerase II alters RNA chain elongation in vitro.” J Biol Chem 260, no. 24 (October 25, 1985): 13190–98.
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  - Biggs, J., L. L. Searles, and A. L. Greenleaf. “Structure of the eukaryotic transcription apparatus: features of the gene for the largest subunit of Drosophila RNA polymerase II.” Cell 42, no. 2 (September 1985): 611–21. https://doi.org/10.1016/0092-8674(85)90118-7.
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  - COULTER, D. E., and A. L. GREENLEAF. “A MUTATION IN THE LARGEST SUBUNIT OF RNA POLYMERASE-II ALTERS RNA CHAIN ELONGATION INVITRO.” Journal of Biological Chemistry 260, no. 24 (January 1, 1985): 3190–98.
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  - Voelker, R. A., A. L. Greenleaf, H. Gyurkovics, G. B. Wisely, S. M. Huang, and L. L. Searles. “Frequent Imprecise Excision among Reversions of a P Element-Caused Lethal Mutation in Drosophila.” Genetics 107, no. 2 (June 1984): 279–94.
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  - Ingles, C. J., H. J. Himmelfarb, M. Shales, A. L. Greenleaf, and J. D. Friesen. “Identification, molecular cloning, and mutagenesis of Saccharomyces cerevisiae RNA polymerase genes.” Proc Natl Acad Sci U S A 81, no. 7 (April 1984): 2157–61. https://doi.org/10.1073/pnas.81.7.2157.
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  - Robbins, A., W. S. Dynan, A. Greenleaf, and R. Tjian. “Affinity-purified antibody as a probe of RNA polymerase II subunit structure.” J Mol Appl Genet 2, no. 4 (1984): 343–53.
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  - Greenleaf, A. L. “Amanitin-resistant RNA polymerase II mutations are in the enzyme's largest subunit.” J Biol Chem 258, no. 22 (November 25, 1983): 13403–6.
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  - Jaenike, J., D. A. Grimaldi, A. E. Sluder, and A. L. Greenleaf. “agr-Amanitin Tolerance in Mycophagous Drosophila.” Science 221, no. 4606 (July 8, 1983): 165–67. https://doi.org/10.1126/science.221.4606.165.
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  - Ingles, C. J., J. Biggs, J. K. Wong, J. R. Weeks, and A. L. Greenleaf. “Identification of a structural gene for a RNA polymerase II polypeptide in Drosophila melanogaster and mammalian species.” Proc Natl Acad Sci U S A 80, no. 11 (June 1983): 3396–3400. https://doi.org/10.1073/pnas.80.11.3396.
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  - GREENLEAF, A. L. “AMANITIN-RESISTANT RNA POLYMERASE-II MUTATIONS ARE IN THE ENZYMES LARGEST SUBUNIT.” Journal of Biological Chemistry 258, no. 22 (January 1, 1983): 3403–6.
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  - GREENLEAF, A. L., J. BIGGS, R. S. JOKERST, and J. R. WEEKS. “A STRUCTURAL GENE FOR AN RNA POLYMERASE-II SUBUNIT.” Federation Proceedings 42, no. 7 (January 1, 1983): 1805–1805.
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  - VOELKER, R. A., S. M. HUANG, H. GYURKOVICS, G. B. WISELY, P. M. BINGHAM, L. L. SEARLES, R. S. JOKERST, and A. L. GREENLEAF. “CLONING AND GENETIC-ANALYSIS OF HYBRID DYSGENESIS-INDUCED ALLELES AT AN RNA POLYMERASE-II LOCUS IN DROSOPHILA-MELANOGASTER.” Environmental Health Perspectives 52, no. OCT (January 1, 1983): 285–285.
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  - Searles, L. L., R. S. Jokerst, P. M. Bingham, R. A. Voelker, and A. L. Greenleaf. “Molecular cloning of sequences from a Drosophila RNA polymerase II locus by P element transposon tagging.” Cell 31, no. 3 Pt 2 (December 1982): 585–92. https://doi.org/10.1016/0092-8674(82)90314-2.
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  - Weeks, J. R., D. E. Coulter, and A. L. Greenleaf. “Immunological studies of RNA polymerase II using antibodies to subunits of Drosophila and wheat germ enzyme.” J Biol Chem 257, no. 10 (May 25, 1982): 5884–92.
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  - Coulter, D. E., and A. L. Greenleaf. “Properties of mutationally altered RNA polymerases II of Drosophila.” J Biol Chem 257, no. 4 (February 25, 1982): 1945–52.
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  - Greenleaf, A. L., J. R. Weeks, R. A. Voelker, S. Ohnishi, and B. Dickson. “Genetic and biochemical characterization of mutants at an RNA polymerase II locus in D. melanogaster.” Cell 21, no. 3 (October 1980): 785–92. https://doi.org/10.1016/0092-8674(80)90441-9.
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  - GREENLEAF, A. L., D. COULTER, J. WEEKS, and R. A. VOELKER. “RNA POLYMERASE-II MUTANTS OF DROSOPHILA.” Federation Proceedings 39, no. 6 (January 1, 1980): 2111–2111.
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  - Greenleaf, A. L., L. M. Borsett, P. F. Jiamachello, and D. E. Coulter. “Alpha-amanitin-resistant D. melanogaster with an altered RNA polymerase II.” Cell 18, no. 3 (November 1979): 613–22. https://doi.org/10.1016/0092-8674(79)90116-8.
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  - Greenleaf, A. L., U. Plagens, M. Jamrich, and E. K. Bautz. “RNA polymerase B (or II) in heat induced puffs of Drosophila polytene chromosomes.” Chromosoma 65, no. 2 (January 16, 1978): 127–36. https://doi.org/10.1007/BF00329465.
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  - Jamrich, M., A. L. Greenleaf, F. A. Bautz, and E. K. Bautz. “Functional organization of polytene chromosomes.” Cold Spring Harb Symp Quant Biol 42 Pt 1 (1978): 389–96. https://doi.org/10.1101/sqb.1978.042.01.040.
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  - Jamrich, M., A. L. Greenleaf, and E. K. Bautz. “Localization of RNA polymerase in polytene chromosomes of Drosophila melanogaster.” Proc Natl Acad Sci U S A 74, no. 5 (May 1977): 2079–83. https://doi.org/10.1073/pnas.74.5.2079.
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  - Jamrich, M., A. L. Greenleaf, F. A. Bautz, and E. K. F. Bautz. “Functional organization of polytene chromosomes.” Cold Spring Harbor Symposia on Quantitative Biology 42, no. 1 (January 1, 1977): 389–96. https://doi.org/10.1101/sqb.1978.042.01.040.
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  - Plagens, U., A. L. Greenleaf, and E. K. Bautz. “Distribution of RNA polymerase on Drosophila polytene chromosomes as studied by indirect immunofluorescence.” Chromosoma 59, no. 2 (December 16, 1976): 157–65. https://doi.org/10.1007/BF00328484.
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  - Greenleaf, A. L., R. Haars, and E. K. Bautz. “In vitro proteolysis of a large subunit of Drosophila melanogaster RNA polymerase B.” Febs Lett 71, no. 2 (December 1, 1976): 205–8. https://doi.org/10.1016/0014-5793(76)80932-5.
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  - Linn, T., A. L. Greenleaf, and R. Losick. “RNA polymerase from sporulating Bacillus subtilis. Purification and properties of a modified form of the enzyme containing two sporulation polypeptides.” J Biol Chem 250, no. 24 (December 25, 1975): 9256–61.
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  - Greenleaf, A. L., and E. K. Bautz. “RNA polymerase B from Drosophila melanogaster larvae. Purification and partial characterization.” Eur J Biochem 60, no. 1 (December 1, 1975): 169–79. https://doi.org/10.1111/j.1432-1033.1975.tb20989.x.
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  - Greenleaf, A. L., and R. Losick. “Appearance of a ribonucleic acid polymerase-binding protein in asporogenous mutants of Bacillus subtilis.” J Bacteriol 116, no. 1 (October 1973): 290–94. https://doi.org/10.1128/JB.116.1.290-294.1973.
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  - Linn, T. G., A. L. Greenleaf, R. G. Shorenstein, and R. Losick. “Loss of the sigma activity of RNA polymerase of Bacillus subtilis during sporulation.” Proc Natl Acad Sci U S A 70, no. 6 (June 1973): 1865–69. https://doi.org/10.1073/pnas.70.6.1865.
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  - Greenleaf, A. L., T. G. Linn, and R. Losick. “Isolation of a new RNA polymerase-binding protein from sporulating Bacillus subtilis.” Proc Natl Acad Sci U S A 70, no. 2 (February 1973): 490–94. https://doi.org/10.1073/pnas.70.2.490.
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  - Rowley, G. L., A. L. Greenleaf, and G. L. Kenyon. “On the specificity of creatine kinase. New glycocyamines and glycocyamine analogs related to creatine.” J Am Chem Soc 93, no. 12 (October 20, 1971): 5542–51. https://doi.org/10.1021/ja00750a038.
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- Conference Papers
  - Liu, Jiangxin, Shilong Fan, Chul-Jin Lee, Arno L. Greenleaf, and Pei Zhou. “Specific interaction of the TCERG1 FF4-6 tandem repeat domains with RNA polymerase II requires simultaneous phosphorylation at Ser2, Ser5 and Ser7 of the CTD.” In Faseb Journal, Vol. 27. FEDERATION AMER SOC EXP BIOL, 2013.
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  - MacKellar, April Lee, and Arno L. Greenleaf. “Association of mRNA export factor Yra1 with the C-terminal Domain of RNA Polymerase II: a mechanism for cotranscriptional recruitment.” In Faseb Journal, Vol. 25. FEDERATION AMER SOC EXP BIOL, 2011.
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  - Greenleaf, A. L., H. P. Phatnani, M. Li, and P. Zhou. “Structure and CTD phosphorylation pattern-binding specificity of the SRI domain of Set2.” In Faseb Journal, 20:A467–A467. FEDERATION AMER SOC EXP BIOL, 2006.
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