A DNA Damage-Induced, SOS-Independent Checkpoint Regulates Cell Division in Caulobacter crescentus

Modell, Joshua W.; Kambara, Tracy K.; Perchuk, Barrett S.; Laub, Michael T.

doi:10.1371/journal.pbio.1001977

Cited by 115 publications

(180 citation statements)

References 53 publications

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“…Several mutations in C. cresentus ftsW have been isolated as hyperactive division mutations (40). Strikingly, our ftsW M269I is adjacent to the corresponding residue of the most potent one (ftsW A246T ) (40). These observations suggest that the domain where these mutations are located has a critical role in FtsW function in divisome activation.…”

Section: Discussionmentioning

confidence: 63%

“…Finally, isolation of ftsW M269I as a hyperactive division mutation suggests that FtsW, along with the FtsQLB complex, plays an important role in keeping the divisome inactive before FtsN arrives at the Z ring. Several mutations in C. cresentus ftsW have been isolated as hyperactive division mutations (40). Strikingly, our ftsW M269I is adjacent to the corresponding residue of the most potent one (ftsW A246T ) (40).…”

Section: Discussionmentioning

confidence: 81%

“…Interestingly, this residue is next to residue ftsW A270 , which corresponds to residue ftsW A246 of Caulobacter crescentus. Mutation of this residue in C. crescentus is hyperactive for division because it results in shorter cells (40). This finding implies that ftsW M269I provides resistance to FtsE D162N X through a similar mechanism as the ftsB and ftsL mutations.…”

Section: Isolation Of Additional Division Protein Mutants That Providementioning

confidence: 95%

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FtsEX acts on FtsA to regulate divisome assembly and activity

Pichoff

Lutkenhaus

2016

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

119

203

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Bacterial cell division is driven by the divisome, a ring-shaped protein complex organized by the bacterial tubulin homolog FtsZ. Although most of the division proteins in Escherichia coli have been identified, how they assemble into the divisome and synthesize the septum remains poorly understood. Recent studies suggest that the bacterial actin homolog FtsA plays a critical role in divisome assembly and acts synergistically with the FtsQLB complex to regulate the activity of the divisome. FtsEX, an ATP-binding cassette transporter-like complex, is also necessary for divisome assembly and inhibits division when its ATPase activity is inactivated. However, its role in division is not clear. Here, we find that FtsEX acts on FtsA to regulate both divisome assembly and activity. FtsX interacts with FtsA and this interaction is required for divisome assembly and inhibition of divisome function by ATPase mutants of FtsEX. Our results suggest that FtsEX antagonizes FtsA polymerization to promote divisome assembly and the ATPase mutants of FtsEX block divisome activity by locking FtsA in the inactive form or preventing FtsA from communicating with other divisome proteins. Because FtsEX is known to govern cell wall hydrolysis at the septum, our findings indicate that FtsEX acts on FtsA to promote divisome assembly and to coordinate cell wall synthesis and hydrolysis at the septum. Furthermore, our study provides evidence that FtsA mutants impaired for self-interaction are favored for division, and FtsW plays a critical role in divisome activation in addition to the FtsQLB complex.

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Section: Discussionmentioning

confidence: 63%

Section: Discussionmentioning

confidence: 81%

Section: Isolation Of Additional Division Protein Mutants That Providementioning

confidence: 95%

See 1 more Smart Citation

FtsEX acts on FtsA to regulate divisome assembly and activity

Pichoff

Lutkenhaus

2016

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

119

203

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“…crescentus also has an SOS-independent, but still DNA damage-induced, response mediated by the transcription factor DriD (Modell et al, 2014). To test whether this pathway was activated by a single DSB, we also assessed the induction of a YFP reporter driven by the didA promoter (Modell et al, 2014).…”

Section: Reca Is Required For Long-range Movement Of Damaged Loci Butmentioning

confidence: 99%

Rapid pairing and resegregation of distant homologous loci enables double-strand break repair in bacteria

Badrinarayanan¹,

Le²,

Laub³

2015

J Exp Med

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“…There is no homolog of ZipA in C. crescentus; instead, the interaction of the Z-ring with the inner membrane in the first stages of divisome assembly seems to be mediated by other proteins, such as the membrane-associated protein FzlC (36,37). It has been recently proposed that the activation of the divisome also occurs in C. crescentus, since point mutations in FtsW, FtsN, and FtsI cause premature division (38,39). In this work, we describe a new conserved protein essential for cell division in C. crescentus.…”

mentioning

confidence: 99%

A New Essential Cell Division Protein in Caulobacter crescentus

et al. 2017

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Bacterial cell division is a complex process that relies on a multiprotein complex composed of a core of widely conserved and generally essential proteins and on accessory proteins that vary in number and identity in different bacteria. The assembly of this complex and, particularly, the initiation of constriction are regulated processes that have come under intensive study. In this work, we characterize the function of DipI, a protein conserved in Alphaproteobacteria and Betaproteobacteria that is essential in Caulobacter crescentus. Our results show that DipI is a periplasmic protein that is recruited late to the division site and that it is required for the initiation of constriction. The recruitment of the conserved cell division proteins is not affected by the absence of DipI, but localization of DipI to the division site occurs only after a mature divisome has formed. Yeast two-hybrid analysis showed that DipI strongly interacts with the FtsQLB complex, which has been recently implicated in regulating constriction initiation. A possible role of DipI in this process is discussed.IMPORTANCE Bacterial cell division is a complex process for which most bacterial cells assemble a multiprotein complex that consists of conserved proteins and of accessory proteins that differ among bacterial groups. In this work, we describe a new cell division protein (DipI) present only in a group of bacteria but essential in Caulobacter crescentus. Cells devoid of DipI cannot constrict. Although a mature divisome is required for DipI recruitment, DipI is not needed for recruiting other division proteins. These results, together with the interaction of DipI with a protein complex that has been suggested to regulate cell wall synthesis during division, suggest that DipI may be part of the regulatory mechanism that controls constriction initiation.KEYWORDS Caulobacter crescentus, SH3 domain, bacterial cell division, constriction initiation, divisome B acterial cell division is a complex process involving the action of a multiprotein complex known as the divisome (1, 2). In Escherichia coli, the divisome is composed of approximately 30 proteins that assemble into a complex spanning from the cytoplasm to the outer membrane (OM). Of these proteins, only 12 are essential in E. coli and 11 are widely conserved in other bacteria, suggesting that they constitute the core of the divisome (3, 4). The divisome complex starts assembling when a ring formed by the FtsZ protein is stabilized at the site where division will occur (5, 6). FtsZ is a tubulin-related cytoplasmic protein that is brought near the cytoplasmic membrane through its interactions with the membrane-associated protein FtsA and, in E. coli, the transmembrane protein ZipA (7,8). The FtsZ ring generates a force sufficient to deform lipid membranes and probably drives the constriction of the inner membrane (9, 10). After establishment of the FtsZ ring, the FtsEX complex is recruited through the interaction of FtsE with FtsZ (11). The divisome then expands to the peripla...

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A DNA Damage-Induced, SOS-Independent Checkpoint Regulates Cell Division in Caulobacter crescentus

Abstract: A study of the bacterium Caulobacter crescentus reveals an SOS-independent DNA damage response pathway that acts via a novel cell division inhibitor, DidA, to suppress septum synthesis.

Cited by 115 publications

References 53 publications

FtsEX acts on FtsA to regulate divisome assembly and activity

FtsEX acts on FtsA to regulate divisome assembly and activity

Rapid pairing and resegregation of distant homologous loci enables double-strand break repair in bacteria

A New Essential Cell Division Protein in Caulobacter crescentus

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