ArticleJournal of bacteriology1999
Membrane-bound division proteins DivIB and DivIC of Bacillus subtilis function solely through their external domains in both vegetative and sporulation division.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Penicillin-binding proteins exhibit functional redundancy during asymmetric cell division inJournal of bacteriology · 2025Article
- SpoIIE drives asymmetric cell division inbioRxiv : the preprint server for biology · 2025Article
- Control of morphogenesis during theScience advances · 2025Article
- Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile.Nature communications · 2023Article
- The Staphylococcus aureus cell division protein, DivIC, interacts with the cell wall and controls its biosynthesis.Communications biology · 2022Article
- Delineating FtsQ-mediated regulation of cell division inThe Journal of biological chemistry · 2018Article
- A role for the essential YycG sensor histidine kinase in sensing cell division.Molecular microbiology · 2011Article
- LAB-Secretome: a genome-scale comparative analysis of the predicted extracellular and surface-associated proteins of Lactic Acid Bacteria.BMC genomics · 2010Article
- Central domain of DivIB caps the C-terminal regions of the FtsL/DivIC coiled-coil rod.The Journal of biological chemistry · 2009Article
- Artificial septal targeting of Bacillus subtilis cell division proteins in Escherichia coli: an interspecies approach to the study of protein-protein interactions in multiprotein complexes.Journal of bacteriology · 2008Article
- Roles of pneumococcal DivIB in cell division.Journal of bacteriology · 2008Article
- LocateP: genome-scale subcellular-location predictor for bacterial proteins.BMC bioinformatics · 2008Article
- Streptomyces coelicolor genes ftsL and divIC play a role in cell division but are dispensable for colony formation.Journal of bacteriology · 2007Article
- Requirement for the cell division protein DivIB in polar cell division and engulfment during sporulation in Bacillus subtilis.Journal of bacteriology · 2006Article
- Domain architecture and structure of the bacterial cell division protein DivIB.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Backbone and side-chain 1H, 15N, and 13C assignments for the beta domain of the bacterial cell division protein DivIB.Journal of biomolecular NMR · 2005Article
- Protein sequences and cellular factors required for polar localization of a histidine kinase in Caulobacter crescentus.Journal of bacteriology · 2002Article
- Analysis of ftsQ mutant alleles in Escherichia coli: complementation, septal localization, and recruitment of downstream cell division proteins.Journal of bacteriology · 2002Article
- Analysis of the essential cell division gene ftsL of Bacillus subtilis by mutagenesis and heterologous complementation.Journal of bacteriology · 2000Article
- Septal localization of the membrane-bound division proteins of Bacillus subtilis DivIB and DivIC is codependent only at high temperatures and requires FtsZ.Journal of bacteriology · 2000Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Bacillus subtilis membrane-bound division proteins, DivIB and DivIC, each contain a single transmembrane segment flanked by a short cytoplasmic N-terminal domain and a larger external C-terminal domain. Both proteins become localized at the division site prior to septation. Mutagenesis of both divIB and divIC was performed whereby the sequences encoding the cytoplasmic domains were replaced by the corresponding sequence of the other gene. Finally, the cytoplasmic-plus-transmembrane-encoding domain of each protein was replaced by a totally foreign sequence not involved in division, that encodes the N-terminal-plus-transmembrane domains of the Escherichia coli TolR protein. B. subtilis strains expressing the divIB and divIC hybrids, in the absence of the wild-type gene, were viable when grown under conditions in which the wild-type genes were found previously to be essential. Furthermore, these strains were able to sporulate to near normal levels. Thus, the cytoplasmic and transmembrane segments of DivIB and DivIC do not appear to have any specific functions other than to anchor these proteins correctly in the membrane. The implications of these findings are discussed.
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