ArticleThe Journal of biological chemistry2009
Central domain of DivIB caps the C-terminal regions of the FtsL/DivIC coiled-coil rod.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- 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
- MraZ Transcriptionally Controls the Critical Level of FtsL Required for Focusing Z-Rings and Kickstarting Septation in Bacillus subtilis.Journal of bacteriology · 2022Article
- The coiled-coil domain of Escherichia coli FtsLB is a structurally detuned element critical for modulating its activation in bacterial cell division.The Journal of biological chemistry · 2022Article
- The Pneumococcal Divisome: Dynamic Control ofFrontiers in microbiology · 2021Review
- Structural Insights into the FtsQ/FtsB/FtsL Complex, a Key Component of the Divisome.Scientific reports · 2018Article
- Structural Analysis of the Interaction between the Bacterial Cell Division Proteins FtsQ and FtsB.mBio · 2018Article
- Delineating FtsQ-mediated regulation of cell division inThe Journal of biological chemistry · 2018Article
- The FtsLB subcomplex of the bacterial divisome is a tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions.The Journal of biological chemistry · 2018Article
- Screening for transmembrane association in divisome proteins using TOXGREEN, a high-throughput variant of the TOXCAT assay.Biochimica et biophysica acta · 2016Article
- The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity.The Journal of biological chemistry · 2015Article
- The stoichiometric divisome: a hypothesis.Frontiers in microbiology · 2015Article
- Identification of SPOR domain amino acids important for septal localization, peptidoglycan binding, and a disulfide bond in the cell division protein FtsN.Journal of bacteriology · 2013Article
- The transmembrane domains of the bacterial cell division proteins FtsB and FtsL form a stable high-order oligomer.Biochemistry · 2013Article
- Structural organization of FtsB, a transmembrane protein of the bacterial divisome.Biochemistry · 2013Article
- Reconstitution of membrane protein complexes involved in pneumococcal septal cell wall assembly.PloS one · 2013Article
- From the regulation of peptidoglycan synthesis to bacterial growth and morphology.Nature reviews. Microbiology · 2011Review
- A model for the Escherichia coli FtsB/FtsL/FtsQ cell division complex.BMC structural biology · 2011Article
- Evidence from artificial septal targeting and site-directed mutagenesis that residues in the extracytoplasmic β domain of DivIB mediate its interaction with the divisomal transpeptidase PBP 2B.Journal of bacteriology · 2010Article
- Advances in understanding E. coli cell fission.Current opinion in microbiology · 2010Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DivIB(FtsQ), FtsL, and DivIC(FtsB) are enigmatic membrane proteins that are central to the process of bacterial cell division. DivIB(FtsQ) is dispensable in specific conditions in some species, and appears to be absent in other bacterial species. The presence of FtsL and DivIC(FtsB) appears to be conserved despite very low sequence conservation. The three proteins form a complex at the division site, FtsL and DivIC(FtsB) being associated through their extracellular coiled-coil region. We report here structural investigations by NMR, small-angle neutron and x-ray scattering, and interaction studies by surface plasmon resonance, of the complex of DivIB, FtsL, and DivIC from Streptococcus pneumoniae, using soluble truncated forms of the proteins. We found that one side of the "bean"-shaped central beta-domain of DivIB interacts with the C-terminal regions of the dimer of FtsL and DivIC. This finding is corroborated by sequence comparisons across bacterial genomes. Indeed, DivIB is absent from species with shorter FtsL and DivIC proteins that have an extracellular domain consisting only of the coiled-coil segment without C-terminal conserved regions (Campylobacterales). We propose that the main role of the interaction of DivIB with FtsL and DivIC is to help the formation, or to stabilize, the coiled-coil of the latter proteins. The coiled-coil of FtsL and DivIC, itself or with transmembrane regions, could be free to interact with other partners.
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