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Cited by 98Bacterial Genetics and BiotechnologyMicrotubule and mitosis dynamicsBiochemical and Structural Characterization

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A Membrane Protein, EzrA, Regulates Assembly Dynamics of FtsZ by Interacting with the C-Terminal Tail of FtsZ

Singh, Jay Kumar, Makde, Ravindra D., Kumar, Vinay, Panda, Dulal·2007·Biochemistry
DOI 10.1021/bi700710j
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Abstract

FtsZ polymerizes to form a dynamic ring structure called the Z-ring at the midcell of bacteria. EzrA, a membrane protein, has been shown to prevent the formation of aberrant Z-rings in the low GC Gram-positive bacteria by inhibiting FtsZ assembly. In this study, we show that Bacillus subtilis (B. subtilis) EzrA inhibited the assembly and bundling of B. subtilis FtsZ. It increased the critical concentration of FtsZ assembly and depolymerized the preformed FtsZ polymers in vitro. We obtained evidence suggesting that B. subtilis EzrA forms complex with B. subtilis FtsZ in vitro. EzrA was found to bind to FtsZ at a single site with a dissociation constant of 4.3 +/- 0.6 microM. EzrA-FtsZ interaction has a significant electrostatic contribution as apparent from the effect of salt on their binding interactions. To elucidate the site of interaction between EzrA and FtsZ, we deleted 16 amino acid residues from the extreme C-terminal tail of B. subtilis FtsZ, which are conserved in FtsZ orthologues. EzrA did not inhibit the assembly of C-terminal truncated B. subtilis FtsZ. It also did not bind to the C-terminal truncated FtsZ detectably, suggesting that EzrA interacts with FtsZ through its conserved C-terminal tail residues. Further, a 17-residue synthetic peptide (365-382) of the C-terminal tail of FtsZ (CTP17) was used to probe the interaction of EzrA with the C-terminal tail of FtsZ. CTP17 bound to EzrA, inhibited the binding of EzrA to FtsZ, and surmounted the inhibitory effects of EzrA on the assembly of FtsZ in vitro. The data together showed that EzrA binds to the C-terminal tail of FtsZ. FtsA, a positive regulator of FtsZ assembly, is also known to interact with the C-terminal tail of FtsZ. The results indicated an interesting possibility that the assembly dynamics of FtsZ in the Z-ring is regulated by the competition between positive and negative regulators sharing the same binding site on FtsZ.

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  • EzrA prevents aberrant FtsZ Z-ring formation in low GC Gram-positive bacteria closely related to JCVI-syn3A.

    “This protein has been demonstrated to prevent aberrant FtsZ Z-ring formation in low GC Gram-positive bacteria that are closely related to JCVI-syn3A.62”

    From Toward the Complete Functional Characterization of a Minimal Bacterial Proteome (2022) · cites this paper as [62]

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Metadata

Authors
Singh, J. K., Makde, R. D., Kumar, V., & Panda, D.
Affiliations
Bhabha Atomic Research Centre (IN)
Corresponding author
Panda, Dulal
ORCID
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2007-08-24
Volume
46
Issue
38
Pages
11013-11022
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi700710j
OpenAlex
W2015483172
Cited by
98
References
0
Citations by year
2026: 2 · 2025: 3 · 2024: 3 · 2023: 5 · 2022: 4 · 2021: 4 · 2020: 6 · 2019: 5 · 2018: 1 · 2017: 4 · 2016: 9 · 2015: 4 · 2014: 7 · 2013: 11 · 2012: 7
FWCI
3.04
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • DSpace (IIT Bombay) (submittedVersion)
Funders
Bhabha Atomic Research Centre
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords
Ezra, FtsZ, Z-ring, bacterial cell division, C-terminal tail, membrane proteins, protein-protein interaction, critical concentration, depolymerization, FtsA, Bacillus subtilis, electrostatic binding, binding sites
MeSH terms
Amino Acid Sequence, Bacillus subtilis, Bacterial Proteins, Binding Sites, Binding, Competitive, Cell Division, Cytoskeletal Proteins, Cytoskeleton, Guanosine Triphosphate, Hydrolysis, Kinetics, Membrane Proteins, Mutation, Peptides, Protein Binding, Recombinant Fusion Proteins, Gene Expression Regulation, Bacterial, Sequence Deletion, Cytokinesis

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