Skip to main content
Journal cover image

Structures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ.

Publication ,  Journal Article
Schumacher, MA; Zeng, W
Published in: Proc Natl Acad Sci U S A
May 3, 2016

Cell division in most prokaryotes is mediated by FtsZ, which polymerizes to create the cytokinetic Z ring. Multiple FtsZ-binding proteins regulate FtsZ polymerization to ensure the proper spatiotemporal formation of the Z ring at the division site. The DNA-binding protein SlmA binds to FtsZ and prevents Z-ring formation through the nucleoid in a process called "nucleoid occlusion" (NO). As do most FtsZ-accessory proteins, SlmA interacts with the conserved C-terminal domain (CTD) that is connected to the FtsZ core by a long, flexible linker. However, SlmA is distinct from other regulatory factors in that it must be DNA-bound to interact with the FtsZ CTD. Few structures of FtsZ regulator-CTD complexes are available, but all reveal the CTD bound as a helix. To deduce the molecular basis for the unique SlmA-DNA-FtsZ CTD regulatory interaction and provide insight into FtsZ-regulator protein complex formation, we determined structures of Escherichia coli, Vibrio cholera, and Klebsiella pneumonia SlmA-DNA-FtsZ CTD ternary complexes. Strikingly, the FtsZ CTD does not interact with SlmA as a helix but binds as an extended conformation in a narrow, surface-exposed pocket formed only in the DNA-bound state of SlmA and located at the junction between the DNA-binding and C-terminal dimer domains. Binding studies are consistent with the structure and underscore key interactions in complex formation. Combined, these data reveal the molecular basis for the SlmA-DNA-FtsZ interaction with implications for SlmA's NO function and underscore the ability of the FtsZ CTD to adopt a wide range of conformations, explaining its ability to bind diverse regulatory proteins.

Duke Scholars

Altmetric Attention Stats
Dimensions Citation Stats

Published In

Proc Natl Acad Sci U S A

DOI

EISSN

1091-6490

Publication Date

May 3, 2016

Volume

113

Issue

18

Start / End Page

4988 / 4993

Location

United States

Related Subject Headings

  • Protein Subunits
  • Protein Domains
  • Protein Conformation
  • Protein Binding
  • Nucleic Acid Conformation
  • Molecular Docking Simulation
  • Models, Chemical
  • Escherichia coli Proteins
  • DNA-Binding Proteins
  • DNA, Bacterial
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Schumacher, M. A., & Zeng, W. (2016). 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(18), 4988–4993. https://doi.org/10.1073/pnas.1602327113
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.
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, vol. 113, no. 18, May 2016, pp. 4988–93. Pubmed, doi:10.1073/pnas.1602327113.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

EISSN

1091-6490

Publication Date

May 3, 2016

Volume

113

Issue

18

Start / End Page

4988 / 4993

Location

United States

Related Subject Headings

  • Protein Subunits
  • Protein Domains
  • Protein Conformation
  • Protein Binding
  • Nucleic Acid Conformation
  • Molecular Docking Simulation
  • Models, Chemical
  • Escherichia coli Proteins
  • DNA-Binding Proteins
  • DNA, Bacterial