Characterization of the essential cell division gene ftsL (yllD ) of Bacillus subtilis and its role in the assembly of the division apparatus

Daniel, Richard A.; Harry, Elizabeth J.; Katis, V.L.; Wake, R.G.; Errington, Jeff

doi:10.1046/j.1365-2958.1998.00954.x

Cited by 110 publications

(151 citation statements)

References 44 publications

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“…YgbQ of E. coli shows only very weak identity with DivIC (14%), but it seems related through the homology of both to a protein in B. halodurans. The septal localization of DivIC in B. subtilis (22) depends on an FtsL homologue (23), and it is unstable in the absence of FtsL (23), suggesting that the two proteins interact (18). Localization of these Bacillus proteins has not been examined.…”

Section: Discussionmentioning

confidence: 99%

YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae , localizes in codependent fashion with FtsL to the division site

Buddelmeijer

Judson

Boyd

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

108

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YgbQ is a cell division protein in Escherichia coli and Vibrio cholerae. In E. coli the ygbQ gene was discovered as a result of a computer search of the E. coli genome designed to find potential interacting partners for cell division protein FtsL. In V. cholerae, ygbQ was identified as an essential gene by using a transposon that fuses genes to an arabinose promoter. The role of YgbQ in cell division is supported by the following. Cells depleted of YgbQ in both organisms form long filaments, but DNA segregation is not affected. YgbQ localizes to the constriction site in wild-type E. coli cells. Localization of E. coli YgbQ to the constriction site depends on cell division proteins FtsQ and FtsL but not FtsW and FtsI, placing YgbQ in the sequential dependency order of proteins localizing to the division site. Localization of green fluorescent protein-FtsL also depends on YgbQ, indicating that FtsL and YgbQ colocalize to the division site in E. coli. Our results show colocalization of proteins to the bacterial midcell in E. coli and raise the possibility that these proteins interact in a coiled-coil structure.C ell division in bacteria takes place at the midcell and occurs after the DNA has been duplicated and segregated into two daughter nucleoids. In Escherichia coli, this process requires a set of at least nine proteins that localize to the constriction site or septum. These proteins coordinate invagination of the cell membrane, inward growth of the peptidoglycan layer, and, finally, separation of daughter cells. The nine proteins, FtsZ, FtsA, ZipA, FtsK, FtsQ, FtsL, FtsW, FtsI, and FtsN, have been identified largely through genetic approaches. Because no systematic genetic approach for identifying such proteins has been performed or devised, there could be a number of thus-farundiscovered proteins that play a role in cell division. Information is available regarding function for only a few of these proteins (reviewed in refs. 1 and 2).Studies from a number of laboratories have led to a sequential dependency model for the assembly of this group of proteins at the cell septum (3). FtsZ arrives first at the cell septum, providing a scaffold for the recruitment of subsequent proteins. FtsA and ZipA localize to the septum independently of each other, but each depends on the presence of FtsZ for localization. The remaining proteins assemble at midcell in a strictly sequential dependency order as follows: FtsK-FtsQ-FtsL-FtsW-FtsIFtsN. The mechanisms for this order of recruitment are not understood.The work reported here arose from projects with different goals in the Beckwith and Mekalanos laboratories. The Beckwith laboratory has studied cell division in E. coli by focusing attention on three proteins, FtsQ, FtsL, and FtsI. These proteins have similar membrane topologies, i.e., a short amino-terminal domain facing the cytoplasm, a single transmembrane segment, and a carboxyl-terminal domain located in the periplasm. FtsL has a leucine zipper-like motif in its periplasmic domain, indicating that it may form coiled-co...

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Section: Discussionmentioning

confidence: 99%

YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae , localizes in codependent fashion with FtsL to the division site

Buddelmeijer

Judson

Boyd

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

108

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“…B. subtilis appears to have a functional homologue of FtsL. Although the primary sequence similarity is negligible, the protein is a likely homologue on the grounds of similar size and predicted transmembrane topology, division phenotype, and the location of its gene immediately upstream of pbpB (36,37). Mutagenesis of the B. subtilis ftsL gene lent support to the notion that few if any of its residues are critical for function (153) and therefore that its function is more likely to be structural than catalytic.…”

Section: Ftsl/divicmentioning

confidence: 99%

“…It appears that DivIC and FtsL interact to form a heterodimer or -oligomer, on the basis of both yeast two-hybrid experiments and native gel electrophoresis (154). Furthermore, depletion of FtsL results in degradation of DivIC, indicating that formation of an FtsL-DivIC complex could stabilize DivIC (36). Interestingly, FtsL (of B. subtilis) is itself an intrinsically unstable protein (34).…”

Section: Ftsl/divicmentioning

confidence: 99%

Cytokinesis in Bacteria

Errington

Daniel

Scheffers

2003

Microbiol Mol Biol Rev

565

601

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Work on two diverse rod-shaped bacteria, Escherichia coli and Bacillus subtilis, has defined a set of about 10 conserved proteins that are important for cell division in a wide range of eubacteria. These proteins are directed to the division site by the combination of two negative regulatory systems. Nucleoid occlusion is a poorly understood mechanism whereby the nucleoid prevents division in the cylindrical part of the cell, until chromosome segregation has occurred near midcell. The Min proteins prevent division in the nucleoid-free spaces near the cell poles in a manner that is beginning to be understood in cytological and biochemical terms. The hierarchy whereby the essential division proteins assemble at the midcell division site has been worked out for both E. coli and B. subtilis. They can be divided into essentially three classes depending on their position in the hierarchy and, to a certain extent, their subcellular localization. FtsZ is a cytosolic tubulin-like protein that polymerizes into an oligomeric structure that forms the initial ring at midcell. FtsA is another cytosolic protein that is related to actin, but its precise function is unclear. The cytoplasmic proteins are linked to the membrane by putative membrane anchor proteins, such as ZipA of E. coli and possibly EzrA of B. subtilis, which have a single membrane span but a cytoplasmic C-terminal domain. The remaining proteins are either integral membrane proteins or transmembrane proteins with their major domains outside the cell. The functions of most of these proteins are unclear with the exception of at least one penicillin-binding protein, which catalyzes a key step in cell wall synthesis in the division septum

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“…Both ftsL and pbpB are essential for cell division (34). FtsL is an unstable protein (35,36); a decrease in ftsL mRNA levels quickly causes a decrease in FtsL protein and inhibits cell division (37). Conversely, PbpB is likely to be a stable protein.…”

Section: Repression Of An Essential Cell Division Gene Couples Replicmentioning

confidence: 99%

“…Because Z-ring formation is independent of FtsL (37,41), the regulation of cell division exerted by FtsL depletion should act after Z-ring formation. Consistent with this hypothesis, HPUra treatment and DNA damage did not abolish Z-ring formation in yneA-null mutants (data not shown) (4).…”

Section: Repression Of An Essential Cell Division Gene Couples Replicmentioning

confidence: 99%

A transcriptional response to replication status mediated by the conserved bacterial replication protein DnaA

Goranov

Katz

Breier

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

263

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Organisms respond to perturbations in DNA replication. We characterized the global transcriptional response to inhibition of DNA replication in Bacillus subtilis. We focused on changes that were independent of the known recA-dependent global DNA damage (SOS) response. We found that overlapping sets of genes are affected by perturbations in replication elongation or initiation and that this transcriptional response serves to inhibit cell division and maintain cell viability. Approximately 20 of the operons (>50 genes) affected have potential DnaA-binding sites and are probably regulated directly by DnaA, the highly conserved replication initiation protein and transcription factor. Many of these genes have homologues and recognizable DnaA-binding sites in other bacteria, indicating that a DnaA-mediated response, elicited by changes in DNA replication status, may be conserved.DNA replication ͉ transcription ͉ DNA microarrays ͉ Bacillus subtilis

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Characterization of the essential cell division gene ftsL (yllD ) of Bacillus subtilis and its role in the assembly of the division apparatus

Cited by 110 publications

References 44 publications

YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae , localizes in codependent fashion with FtsL to the division site

YgbQ, a cell division protein in Escherichia coli and Vibrio cholerae , localizes in codependent fashion with FtsL to the division site

Cytokinesis in Bacteria

A transcriptional response to replication status mediated by the conserved bacterial replication protein DnaA

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