Structure and function of a spectrin-like regulator of bacterial cytokinesis

Cleverley, Robert M.; Barrett, Jeffrey R.; Baslé, Arnaud; Bui, Nhat Khai; Hewitt, Lorraine; Solovyova, Alexandra; Xu, Zhi-Qiang; Daniel, Richard A.; Dixon, Nicholas E.; Harry, Elizabeth J.; Oakley, Aaron J.; Vollmer, Waldemar; Lewis, Richard J.

doi:10.1038/ncomms6421

Cited by 53Bacterial Genetics and BiotechnologyBiochemical and Structural CharacterizationMicrotubule and mitosis dynamics

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Structure and function of a spectrin-like regulator of bacterial cytokinesis

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Cleverley, Robert M., Barrett, Jeffrey R., Baslé, Arnaud, Bui, Nhat Khai, Hewitt, Lorraine, Solovyova, Alexandra, Xu, Zhi-Qiang, Daniel, Richard A., Dixon, Nicholas E., Harry, Elizabeth J., Oakley, Aaron J., Vollmer, Waldemar, Lewis, Richard J.·2014·Nature Communications

DOI 10.1038/ncomms6421PMC PMC4243239

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Abstract

Bacterial cell division is facilitated by a molecular machine—the divisome—that assembles at mid-cell in dividing cells. The formation of the cytokinetic Z-ring by the tubulin homologue FtsZ is regulated by several factors, including the divisome component EzrA. Here we describe the structure of the 60-kDa cytoplasmic domain of EzrA, which comprises five linear repeats of an unusual triple helical bundle. The EzrA structure is bent into a semicircle, providing the protein with the potential to interact at both N- and C-termini with adjacent membrane-bound divisome components. We also identify at least two binding sites for FtsZ on EzrA and map regions of EzrA that are responsible for regulating FtsZ assembly. The individual repeats, and their linear organization, are homologous to the spectrin proteins that connect actin filaments to the membrane in eukaryotes, and we thus propose that EzrA is the founding member of the bacterial spectrin family.

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Hydrophobic regions at the N and C termini of the AlphaFold2 predicted structure of /0239 match previous findings that EzrA binds the membrane at each terminal domain.
“Hydrophobic regions at the N and C termini match the previous findings that EzrA binds the membrane at each terminal domain.65”
From Toward the Complete Functional Characterization of a Minimal Bacterial Proteome (2022) · cites this paper as [65]
The Results section, “EzrA has a semi-circular structure,” says the N-terminal transmembrane helix embeds EzrA in the membrane, while the C-terminal bundle has the potential to interact with it. The Discussion describes C-terminal membrane interaction as model-dependent and notes an orientation that would place the bundle away from the membrane. The source therefore does not establish that EzrA binds the membrane at both termini, nor does it assess the cited AlphaFold2 structure. (LLM, conf=0.88)
Experimental — accuracy not yet measured
Gene /0239 is ezrA, encoding an FtsZ filament regulator involved in cell division.
“ezrA/0239 | cell division | FtsZ filament regulator”
From Toward the Complete Functional Characterization of a Minimal Bacterial Proteome (2022) · cites this paper as [65]
The paper describes EzrA as a regulator of FtsZ assembly involved in bacterial cell division (Abstract; Results, ‘Effect of EzrA on FtsZ oligomerisation’; page numbers unavailable). Our copy does not identify ezrA as gene /0239, so the gene-number mapping is not supported. (LLM, conf=0.86)
Experimental — accuracy not yet measured
The AlphaFold2 predicted structure of gene /0239 aligns to the experimental structure of EzrA from B. subtilis (PDB 4UXV) with 84% of residues well-aligned and a p-value of 3.01 × 10-10.
“Structural alignment by FATCAT25 of the predicted AlphaFold2 structure for gene /0239 (blue) to the structure of the cell division regulatory protein EzrA from B. subtilis (yellow, RCSB PDB: 4UXV(65)) with 498 or 84% of the residues of /0239 being well-aligned to the experimental structure with a p-value of 3.01 × 10–10 for significant structural similarity.”
From Toward the Complete Functional Characterization of a Minimal Bacterial Proteome (2022) · cites this paper as [65]

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Authors: Cleverley, R. M., Barrett, J. R., Baslé, A., Bui, N. K., Hewitt, L., Solovyova, A., Xu, Z.-Q., Daniel, R. A., Dixon, N. E., Harry, E. J., Oakley, A. J., Vollmer, W., & Lewis, R. J.
Affiliations: Newcastle University (GB)
University of Wollongong (AU)
Helmholtz Centre for Infection Research (DE)
University of Technology Sydney (AU)
Corresponding author: Lewis, Richard J.
ORCID: Barrett, Jeffrey R.
Baslé, Arnaud
Solovyova, Alexandra
Xu, Zhi-Qiang
Daniel, Richard A.
Dixon, Nicholas E.
Harry, Elizabeth J.
Oakley, Aaron J.
Vollmer, Waldemar
Lewis, Richard J.
Venue: Nature Communications
Publisher: Springer Science and Business Media LLC
Published: 2014-11-18
Volume: 5
Issue: 1
Pages: 5421-5421
ISSN: 2041-1723 (ISSN-L)
DOI: 10.1038/ncomms6421
PMC: PMC4243239
OpenAlex: W1969824329
Cited by: 50
References: 71
Citations by year: 2026: 6 · 2025: 4 · 2024: 1 · 2023: 4 · 2022: 3 · 2021: 3 · 2020: 3 · 2019: 7 · 2018: 4 · 2017: 5 · 2016: 5 · 2015: 5
FWCI: 2.60
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0 (tdm)
creativecommons.org/licenses/by/4.0 (vor)
Locations: Nature Communications (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Research Online (University of Wollongong) (submittedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Figshare (submittedVersion)
UTS ePRESS (University of Technology Sydney) (submittedVersion)
Newcastle University ePrints (Newcastle Univesity) (cc-by)
Funders: Diamond Light Source
University of Manchester
Australian Synchrotron
Biotechnology and Biological Sciences Research Council (983409, BB/G015902/1)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords: Ezra, bacterial cytokinesis, divisome, FtsZ, Z-ring, spectrin-like protein, protein structure, cell division machinery
MeSH terms: Bacillus subtilis, Bacterial Proteins, Binding Sites, Cytoskeletal Proteins, Spectrin, Crystallography, X-Ray, Cytokinesis

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Structure and function of a spectrin-like regulator of bacterial cytokinesis

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