The
            <i>Escherichia coli</i>
            Cell Division Protein FtsW Is Required To Recruit Its Cognate Transpeptidase, FtsI (PBP3), to the Division Site

Mercer, Keri L. N.; Weiss, David S.

doi:10.1128/jb.184.4.904-912.2002

Cited by 162 publications

(173 citation statements)

References 46 publications

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“…Interestingly, FtsW and FtsN also interacted strongly with each other, as reported recently in E. coli (Alexeeva et al 2010). Although SidA did not interact with full-length FtsI, neither did FtsW (data not shown), as expected based on studies in E. coli (Mercer and Weiss 2002). We therefore tested a truncated version of FtsI (FtsIDC) lacking its periplasmic catalytic domain.…”

Section: Sida Resides In the Inner Membrane And Interacts Directly Wimentioning

confidence: 93%

A DNA damage checkpoint in Caulobacter crescentus inhibits cell division through a direct interaction with FtsW

Modell¹,

Hopkins²,

Laub³

2011

Genes Dev.

128

200

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Following DNA damage, cells typically delay cell cycle progression and inhibit cell division until their chromosomes have been repaired. The bacterial checkpoint systems responsible for these DNA damage responses are incompletely understood. Here, we show that Caulobacter crescentus responds to DNA damage by coordinately inducing an SOS regulon and inhibiting the master regulator CtrA. Included in the SOS regulon is sidA (SOS-induced inhibitor of cell division A), a membrane protein of only 29 amino acids that helps to delay cell division following DNA damage, but is dispensable in undamaged cells. SidA is sufficient, when overproduced, to block cell division. However, unlike many other regulators of bacterial cell division, SidA does not directly disrupt the assembly or stability of the cytokinetic ring protein FtsZ, nor does it affect the recruitment of other components of the cell division machinery. Instead, we provide evidence that SidA inhibits division by binding directly to FtsW to prevent the final constriction of the cytokinetic ring.

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Section: Sida Resides In the Inner Membrane And Interacts Directly Wimentioning

confidence: 93%

A DNA damage checkpoint in Caulobacter crescentus inhibits cell division through a direct interaction with FtsW

Modell¹,

Hopkins²,

Laub³

2011

Genes Dev.

128

200

View full text Add to dashboard Cite

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“…Prior to its assembly at midcell, C. crescentus FtsZ has been shown to localize at the stalk pole (38). This event makes FtsZ an intriguing candidate as a recruiter of DivJ based on the observation in E. coli that FtsZ is required for the recruitment of FtsA, which in turn is needed to recruit additional division proteins such as FtsN and FtsW (1,24,26,47). Similarly, in B. subtilis, FtsZ is required to recruit the DivIB and DivIC proteins to the division septum (22).…”

Section: Discussionmentioning

confidence: 99%

Protein Sequences and Cellular Factors Required for Polar Localization of a Histidine Kinase in Caulobacter crescentus

et al. 2002

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The Caulobacter crescentus sensor kinase DivJ is required for an early cell division step and localizes at the base of the newly formed stalk during the G 1 -to-S-phase transition when the protein is synthesized. To identify sequences within DivJ that are required for polar localization, we examined the ability of mutagenized DivJ sequences to direct localization of the green fluorescent protein. The effects of overlapping C-terminal deletions of DivJ established that the N-terminal 326 residues, which do not contain the kinase catalytic domain, are sufficient for polar localization of the fusion protein. Internal deletions mapped a shorter sequence between residues 251 and 312 of the cytoplasmic linker that are required for efficient localization of this sensor kinase. PleC kinase mutants, which are blocked in the swarmer-to-stalked-cell transition and form flagellated, nonmotile cells, also fail to localize DivJ. To dissect the cellular factors involved in establishing subcellular polarity, we have examined DivJ localization in a pleC mutant suppressed by the sokA301 allele of ctrA and in a pleD mutant, both of which display a supermotile, stalkless phenotype. The observation that these Mot ؉ strains localize DivJ to a single cell pole indicate that localization may be closely coupled to the gain of motility and that normal stalk formation is not required. We have also observed, however, that filamentous parC mutant cells, which are defective in DNA segregation and the completion of cell separation, are motile and still fail to localize DivJ to the new cell pole. These results suggest that formation of new sites for DivJ localization depends on events associated with the completion of cell separation as well as the gain of motility. Analysis of PleC and PleD mutants also provides insights into the function of the His-Asp proteins in cell cycle regulation. Thus, the ability of the sokA301 allele of ctrA to bypass the nonmotile phenotype of the pleC null mutation provides evidence that the PleC kinase controls cell motility by initiating a signal transduction pathway regulating activity of the global response regulator CtrA. Analysis of the pleD mutant cell cycle demonstrates that disruption of the swarmer-to-stalked-cell developmental sequence does not affect the asymmetric organization of the Caulobacter cell cycle.

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“…Immunofluorescence microscopy has shown that in E. coli during the later stages of cell growth FtsI localizes to the division site at the septum. The septal localization of FtsI, however, depends upon prior localization of the other cell division proteins, such as FtsZ, FtsA, FtsK, FtsQ, FtsL and FtsW (Mercer & Weiss, 2002;Weiss et al, 1999), and therefore, it appears that FtsI is a late recruit to the division site. In B. subtilis, the septal localization of PBP3/FtsI is also delayed, but is needed for the localization of the division inhibitor MinC (Marston & Errington, 1999).…”

Section: Introductionmentioning

confidence: 99%

Morphological changes and proteome response of Corynebacterium glutamicum to a partial depletion of FtsI

et al. 2006

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In Corynebacterium glutamicum, as in many Gram-positive bacteria, the cell division gene ftsI is located at the beginning of the dcw cluster, which comprises cell division-and cell wall-related genes. Transcriptional analysis of the cluster revealed that ftsI is transcribed as part of a polycistronic mRNA, which includes at least mraZ, mraW, ftsL, ftsI and murE, from a promoter that is located upstream of mraZ. ftsI appears also to be expressed from a minor promoter that is located in the intergenic ftsL-ftsI region. It is an essential gene in C. glutamicum, and a reduced expression of ftsI leads to the formation of larger and filamentous cells. A translational GFP-FtsI fusion protein was found to be functional and localized to the mid-cell of a growing bacterium, providing evidence of its role in cell division in C. glutamicum. This study involving proteomic analysis (using 2D SDS-PAGE) of a C. glutamicum strain that has partially depleted levels of FtsI reveals that at least 20 different proteins were overexpressed in the organism. Eight of these overexpressed proteins, which include DivIVA, were identified by MALDI-TOF. Overexpression of DivIVA was confirmed by Western blotting using anti-DivIVA antibodies, and also by fluorescence microscopy analysis of a C. glutamicum RESF1 strain expressing a chromosomal copy of a divIVA-gfp transcriptional fusion. Overexpression of DivIVA was not observed when FtsI was inhibited by cephalexin treatment or by partial depletion of FtsZ.

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The Escherichia coli Cell Division Protein FtsW Is Required To Recruit Its Cognate Transpeptidase, FtsI (PBP3), to the Division Site

Cited by 162 publications

References 46 publications

A DNA damage checkpoint in Caulobacter crescentus inhibits cell division through a direct interaction with FtsW

A DNA damage checkpoint in Caulobacter crescentus inhibits cell division through a direct interaction with FtsW

Protein Sequences and Cellular Factors Required for Polar Localization of a Histidine Kinase in Caulobacter crescentus

Morphological changes and proteome response of Corynebacterium glutamicum to a partial depletion of FtsI

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