The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
Abstract
Summary: The cytokinetic Z ring is required for bacterial cell division. It consists of polymers of FtsZ, the bacterial ancestor of eukaryotic tubulin, linked to the cytoplasmic membrane. Formation of a Z ring in Escherichia coli occurs as long as one of two proteins, ZipA or FtsA, is present. Both of these proteins bind FtsZ suggesting that they might function to tether FtsZ filaments to the membrane. Although ZipA has a transmembrane domain and therefore can function as a membrane anchor, interaction of FtsA with the membrane has not been explored. In this study we demonstrate that FtsA, which is structurally related to eukaryotic actin, has a conserved C‐terminal amphipathic helix that is essential for FtsA function. It is required to target FtsA to the membrane and subsequently to the Z ring. As FtsA is much more widely conserved in bacteria than ZipA, it is likely that FtsA serves as the principal membrane anchor for the Z ring.
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Citations
Cites
Assembly Dynamics of the Bacterial Cell Division Protein FtsZ: Poised at the Edge of Stability
Romberg, L., & Levin, P. A. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.012903.074300 · Cited by 260
Cited by
The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns
Loose, M., & Mitchison, T. J. (2014) · Nature Cell Biology · doi:10.1038/ncb2885 · Cited by 378
Shih, Y.-L., & Rothfield, L. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00017-06 · Cited by 266
FtsA forms actin‐like protofilaments
Szwedziak, P., Wang, Q., Freund, S. M., & Löwe, J. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.76 · Cited by 233
SepF, a novel FtsZ‐interacting protein required for a late step in cell division
Hamoen, L. W., Meile, J., De Jong, W., Noirot, P., & Errington, J. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04987.x · Cited by 180
Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring
Duman, R., Ishikawa, S., Celik, I., Strahl, H., Ogasawara, N., Troc, P., Löwe, J., & Hamoen, L. W. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313978110 · Cited by 150
Metadata
- Authors
- Pichoff, S., & Lutkenhaus, J.
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2005-02-04
- Volume
- 55
- Issue
- 6
- Pages
- 1722-1734
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W1505479679
- Cited by
- 439
- References
- 1
- FWCI
- 11.26
- Type
- journal article
- Language
- en
- Open access
- closed
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- Pichoff, S., & Lutkenhaus, J. (2005). Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Molecular Microbiology. https://doi.org/10.1111/j.1365-2958.2005.04522.x
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
