Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in <i>Bacillus subtilis</i>

Leaver, Mark; Errington, Jeff

doi:10.1111/j.1365-2958.2005.04736.x

Cited by 157 publications

(218 citation statements)

References 40 publications

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“…The shape defect was seen when cells were depleted in CH or PAB medium, but not in S medium. Recently, we have reported that normal growth of mreB, mreC and mreD, which are required for controlling cell shape, can be restored by the addition of magnesium to the medium (Formstone & Errington, 2005;Leaver & Errington, 2005). However, this is not the case for ylaN, suggesting that cells depleted for YlaN have lost the ability to control some aspect of growth or cell wall synthesis that is distinct from that operated on by the Mre proteins.…”

Section: Effects On Morphology Following Depletion Of Essential Proteinsmentioning

confidence: 74%

Functional analysis of 11 putative essential genes in Bacillus subtilis

et al. 2006

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Systematic inactivation of Bacillus subtilis genes has previously revealed that 271 are indispensable for growth. In the present study, 11 of these (yacA, ydiB, ydiC, ykqC, ylaN, yloQ, ymdA, yneS, yqeI, yqjK and ywlC) were identified as genes encoding proteins of unknown function. By analysing the effects of protein depletion, and examining the subcellular localization of these proteins, a start has been made in elucidating their functions. It was found that four of these genes (ydiB, yloQ, yqeI and ywlC) were not required for B. subtilis viability. Analysis of the localization of YkqC suggests that it co-localizes with ribosomes, and it is proposed that it is involved in processing either rRNA or specific mRNAs when they are associated with the ribosome. The results suggest that other novel essential proteins may be involved in lipid synthesis and control of cell wall synthesis.

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Section: Effects On Morphology Following Depletion Of Essential Proteinsmentioning

confidence: 74%

Functional analysis of 11 putative essential genes in Bacillus subtilis

et al. 2006

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“…How this occurs is not fully understood, but other proteins of the core morphogenic apparatus, such as MreC, MreD, and RodA are likely to be involved. While the exact function of these membrane-bound or periplasmic proteins remains somewhat unclear, evidence suggests that they regulate PG growth by linking MreB to cell wall enzymes or by working in concert with MreB to spatially restrict cell wall activities (9)(10)(11)(12)(13)(14)(15)(16)(17).…”

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confidence: 99%

RodZ, a component of the bacterial core morphogenic apparatus

Alyahya

Alexander

Costa

et al. 2009

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

162

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“…MreB homologs are known to form helices in E. coli, B. subtilis,[15][16][17][18]. Therefore, a reasonable hypothesis is that MreB ensures a helical pattern of cell wall growth during elongation by directly positioning the peptidoglycan precursors along its own spiral scaffold; however, there is not yet any direct evidence for an interaction between the peptidoglycan (or any of its modifying enzymes) and MreB.MreB is thought to act with the coexpressed MreC protein to regulate cell shape (10,19,20). MreC resides primarily external to the cytoplasmic membrane, anchored by a single transmembrane domain near the N terminus (19).…”

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confidence: 99%

“…MreB is thought to act with the coexpressed MreC protein to regulate cell shape (10,19,20). MreC resides primarily external to the cytoplasmic membrane, anchored by a single transmembrane domain near the N terminus (19).…”

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Two independent spiral structures control cell shape inCaulobacter

Dye

Pincus

Theriot

et al. 2005

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

123

158

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The actin homolog MreB contributes to bacterial cell shape. Here, we explore the role of the coexpressed MreC protein in Caulobacter and show that it forms a periplasmic spiral that is out of phase with the cytoplasmic MreB spiral. Both mreB and mreC are essential, and depletion of either protein results in a similar cell shape defect. MreB forms dynamic spirals in MreC-depleted cells, and MreC localizes helically in the presence of the MreB-inhibitor A22, indicating that each protein can form a spiral independently of the other. We show that the peptidoglycan transpeptidase Pbp2 also forms a helical pattern that partially colocalizes with MreC but not MreB. Perturbing either MreB (with A22) or MreC (with depletion) causes GFP-Pbp2 to mislocalize to the division plane, indicating that each is necessary but not sufficient to generate a helical Pbp2 pattern. We show that it is the division process that draws Pbp2 to midcell in the absence of MreB's regulation, because cells depleted of the tubulin homolog FtsZ maintain a helical Pbp2 localization in the presence of A22. By developing and employing a previously uncharacterized computational method for quantitating shape variance, we find that a FtsZ depletion can also partially rescue the A22-induced shape deformation. We conclude that MreB and MreC form spatially distinct and independently localized spirals and propose that MreB inhibits division plane localization of Pbp2, whereas MreC promotes lengthwise localization of Pbp2; together these two mechanism ensure a helical localization of Pbp2 and, thereby, the maintenance of proper cell morphology in Caulobacter.actin ͉ MreB ͉ MreC ͉ Pbp2 P rokaryotes exhibit a wide variety of cell shapes (including rods, spheres, spirals, squares, and stars), but the mechanisms by which these shapes are achieved are poorly understood. The extracellular peptidoglycan layer provides structural rigidity for bacterial cells and is of central importance in the establishment and maintenance of cell shape (1, 2). This layer is a meshwork of disaccharide chains (alternating N-acetylglucosamine and N-acetylmuramic acid sugars) cross-linked by short peptide bridges. Rod-shaped bacteria are believed to possess two peptidoglycan synthesis complexes with distinct activities: one for elongation along the cell length and the other for cell division (1, 3, 4). It is thought that maintenance of a regular rod shape requires the activities of these two complexes to be carefully balanced (3).The bacterial cytoskeleton also plays a role in the establishment and maintenance of cell shape (2). Homologs for the three major types of eukaryotic cytoskeletal elements have been identified in bacteria: the actin homolog is MreB, the tubulin homolog, FtsZ, and the intermediate filament homolog, Crescentin (5). Of these known cytoskeletal elements, MreB is the only one required to establish an underlying rod-like character. Mutations in mreB confer a spherical-like morphology to the normally rod-like cells of Escherichia coli, Bacillus subtilis, and Caulobact...

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Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis

Cited by 157 publications

References 40 publications

Functional analysis of 11 putative essential genes in Bacillus subtilis

Functional analysis of 11 putative essential genes in Bacillus subtilis

RodZ, a component of the bacterial core morphogenic apparatus

Two independent spiral structures control cell shape inCaulobacter

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