A temporally controlled sigma-factor is required for polar morphogenesis and normal cell division in Caulobacter.

Brun, Yves V.; Shapiro, Lucille

doi:10.1101/gad.6.12a.2395

Cited by 124 publications

(147 citation statements)

References 37 publications

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“…DNA manipulations, genetic techniques, immunoblotting and cell synchronization General cloning and genetic procedures were as described previously (Brun and Shapiro, 1992). For immunoblotting, total cell lysates were resolved on a SDS-PAGE gel and transferred to nitrocellulose (Schleicher & Schuell).…”

Section: Methodsmentioning

confidence: 99%

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Dominant C‐terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA

Din

Quardokus

Sackett

et al. 1998

Molecular Microbiology

115

116

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SummaryThe cell division protein FtsZ is composed of three regions based on sequence similarity: a highly conserved N-terminal region of Ϸ320 amino acids; a variable spacer region; and a conserved C-terminal region of eight amino acids. We show that FtsZ mutants missing different C-terminal fragments have dominant lethal effects because they block cell division in Caulobacter crescentus by two different mechanisms. Removal of the C-terminal conserved region, the linker, and 40 amino acids from the end of the Nterminal conserved region (FtsZ⌬C281) prevents the localization or the polymerization of FtsZ. Because two-hybrid analysis indicates that FtsZ⌬C281 does not interact with FtsZ, we hypothesize that FtsZ⌬C281 blocks cell division by competing with a factor required for FtsZ localization or that it titrates a factor required for the stability of the FtsZ ring. The removal of 24 amino acids from the C-terminus of FtsZ (FtsZ⌬C485) causes a punctate pattern of FtsZ localization and affects its interaction with FtsA. This suggests that the conserved C-terminal region of FtsZ is required for proper polymerization of FtsZ in Caulobacter and for its interaction with FtsA.

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Section: Methodsmentioning

confidence: 99%

“…Cells were washed again with PBS and treated with SlowFade (Molecular Probes) before applying a coverslip. Transmission electron microscopy (TEM) was performed as described (Brun and Shapiro, 1992) using a JOEL JEM-1010 electron microscope at 60 kV. Whole-cell mounts were stained with a 7.5% uranyl magnesium acetate from Ted Pella.…”

Section: Microscopymentioning

confidence: 99%

Dominant C‐terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA

Din

Quardokus

Sackett

et al. 1998

Molecular Microbiology

115

116

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“…This observation may be due to pleiotropic or polar effects, as one of these insertions lies within the gene encoding the alternative sigma factor RpoN. It is reasonable to suspect that RpoN is required for motility-gene expression in V. anguillarum, as it is in other bacteria including Vibrio cholerae, Pseudomonas aeruginosa and Caulobacter crescentus (Klose and Mekalanos, 1996;Totten et al, 1990;Brun and Shapiro, 1992). RpoN may also control expression of non-motility-associated virulence factors required for pathogenesis.…”

Section: Glowing Squid Septic Trout and Aquatic Vibriosmentioning

confidence: 99%

Roles for motility in bacterial–host interactions

Ottemann

Miller

1997

Molecular Microbiology

286

217

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SummaryThe ability to move in a directed manner may confer distinct advantages upon host-adapted prokaryotes. Potential benefits of motility include increased efficiency of nutrient acquisition, avoidance of toxic substances, the ability to translocate to preferred hosts and access optimal colonization sites within them, and dispersal in the environment during the course of transmission. The costs of motility also may be significant. These include the metabolic burden of synthesizing flagellar components, the energetic expense of fuelling flagellar motors and the presentation of polymeric and highly antigenic targets to the immune system. It is therefore not surprising that synthesis of the motility apparatus is usually subject to strict control. Studies of a variety of bacterial-host interactions demonstrate roles for motility, and its regulation, at points throughout the infectious cycle.

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“…The alternative sigma factor s 54 (encoded by rpoN) and the response regulator TacA direct the transcription of genes needed for stalk biogenesis, and rpoN and tacA mutants are stalkless in rich medium (Biondi et al, 2006;Brun & Shapiro, 1992;Skerker et al, 2005). However, the need for s 54 and TacA can be overcome by growing cells in low-phosphate medium (Biondi et al, 2006;Brun & Shapiro, 1992). Under these conditions, a second regulatory pathway, possibly mediated by the response regulator PhoB, promotes stalk outgrowth (Gonin et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane β-barrel proteins in Caulobacter crescentus

2010

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The outer membrane of Gram-negative bacteria is an essential compartment containing a specific complement of lipids and proteins that constitute a protective, selective permeability barrier. Outer membrane β-barrel proteins are assembled into the membrane by the essential hetero-oligomeric BAM complex, which contains the lipoprotein BamE. We have identified a homologue of BamE, encoded by CC1365, which is located in the outer membrane of the stalked alpha-proteobacterium Caulobacter crescentus. BamE associates with proteins whose homologues in other bacteria are known to participate in outer membrane protein assembly: BamA (CC1915), BamB (CC1653) and BamD (CC1984). Caulobacter cells lacking BamE grow slowly in rich medium and are hypersensitive to anionic detergents, some antibiotics and heat exposure, which suggest that the membrane integrity of the mutant is compromised. Membranes of the ΔbamE mutant have normal amounts of the outer membrane protein RsaF, a TolC homologue, but are deficient in CpaC*, an aggregated form of the outer membrane secretin for type IV pili. ΔbamE membranes also contain greatly reduced amounts of three TonB-dependent receptors that are abundant in wild-type cells. Cells lacking BamE have short stalks and are delayed in stalk outgrowth during the cell cycle. Based on these findings, we propose that Caulobacter BamE participates in the assembly of outer membrane β-barrel proteins, including one or more substrates required for the initiation of stalk biogenesis.

show abstract

A temporally controlled sigma-factor is required for polar morphogenesis and normal cell division in Caulobacter.

Cited by 124 publications

References 37 publications

Dominant C‐terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA

Dominant C‐terminal deletions of FtsZ that affect its ability to localize in Caulobacter and its interaction with FtsA

Roles for motility in bacterial–host interactions

The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane β-barrel proteins in Caulobacter crescentus

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