The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site
Open accessAbstract
Cell division in rod-shaped bacteria is initiated by formation of a ring of the tubulin-like protein FtsZ at mid-cell. Division site selection is controlled by a conserved division inhibitor MinCD, which prevents aberrant division at the cell poles. The Bacillus subtilis DivIVA protein controls the topological specificity of MinCD action. Here we show that DivIVA is targeted to division sites late in their assembly, after some MinCD-sensitive step requiring FtsZ and other division proteins has been passed. DivIVA then recruits MinD to the division sites preventing another division from taking place near the newly formed cell poles. Sequestration of MinD to the poles also releases the next mid-cell sites for division. Remarkably, this mechanism of DivIVA action is completely different from that of the equivalent protein MinE of Escherichia coli, even though both systems operate via the same division inhibitor MinCD.
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Self-citationFtsZ and the division of prokaryotic cells and organelles
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Self-citationThe Spo0A regulon of Bacillus subtilis
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Metadata
- Authors
- Marston, A. L., Thomaides, H. B., Edwards, D. H., Sharpe, M. E., & Errington, J.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1998-11-01
- Volume
- 12
- Issue
- 21
- Pages
- 3419-3430
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2100311602
- Cited by
- 377
- References
- 53
- Type
- posted content
- Language
- en
- Open access
- diamond
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- Marston, A. L., Thomaides, H. B., Edwards, D. H., Sharpe, M. E., & Errington, J. (1998). Polar localization of the MinD protein of Bacillus subtilis and its role in selection of the mid-cell division site. Genes & Development. https://doi.org/10.1101/gad.12.21.3419
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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