Overview of cell shape: cytoskeletons shape bacterial cells

Pichoff, Sébastien; Lutkenhaus, Joe

doi:10.1016/j.mib.2007.09.005

Cited by 27 publications

(18 citation statements)

References 41 publications

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“…7c and d, respectively, for phase contrast and scanning electron micrographs). In rod-shaped bacteria, the peptidoglycan layer both prevents osmotic lysis and maintains the bacilloid morphology, the natural lowest energy form being coccoid (Pichoff and Lutkenhaus 2007). Presumably, the addition of NaCl reduced the pressure on the cells to lyse, without affecting the pressure-independent collapse to spheroplasts.…”

Section: Resultsmentioning

confidence: 99%

Lytic enzyme discovery through multigenomic sequence analysis in Clostridium perfringens

Schmitz

Ossiprandi

Rumah

et al. 2010

Appl Microbiol Biotechnol

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With their ability to lyse Gram-positive bacteria, phage lytic enzymes (or lysins) have received a great deal of attention as novel anti-infective agents. The number of known genes encoding these peptidoglycan hydrolases has increased markedly in recent years, due in large part to advances in DNA sequencing technology. As the genomes of more and more bacterial species/strains are sequenced, lysin-encoding open reading frames (ORFs) can be readily identified in lysogenized prophage regions. In the current study, we sought to assess lysin diversity for the medically relevant pathogen Clostridium perfringens. The sequenced genomes of nine C. perfringens strains were computationally mined for prophage lysins and lysin-like ORFs, revealing several dozen proteins of various enzymatic classes. Of these lysins, a muramidase from strain ATCC 13124 (termed PlyCM) was chosen for recombinant analysis based on its dissimilarity to previously characterized C. perfringens lysins. Following expression and purification, various biochemical properties of PlyCM were determined in vitro, including pH/salt-dependence and temperature stability. The enzyme exhibited activity at low µg/ml concentrations, a typical value for phage lysins. It was active against 23 of 24 strains of C. perfringens tested, with virtually no activity against other clostridial or nonclostridial species. Overall, PlyCM shows potential for development as an enzybiotic agent, demonstrating how expanding genomic databases can serve as rich pools for biotechnologically relevant proteins.

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Section: Resultsmentioning

confidence: 99%

Lytic enzyme discovery through multigenomic sequence analysis in Clostridium perfringens

Schmitz

Ossiprandi

Rumah

et al. 2010

Appl Microbiol Biotechnol

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“…In bacteria, some cell shape factors are limited to certain species or subsets, such as teichoic acids in gram-positive bacteria or crescentin in Caulobacter crescentus. However, there is also a core morphogenic apparatus composed of proteins with a broad, more universal function, and among them, the cytoskeleton plays a central role (1)(2)(3). This apparatus primarily dictates cell shape by topological control of cell growth.…”

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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

219

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“…The FtsZ tubulin homolog plays a critical role in cell division by assembling into a ring structure that constricts during cytokinesis (Margolin 2006;Pichoff and Lutkenhaus 2007). The FtsZ ring is highly dynamic (Ben-Yehuda and Losick 2002;Thanedar and Margolin 2004;Peters et al 2007) and exchanges subunits with the cytoplasmic pool on time scales of seconds (Anderson et al 2004).…”

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confidence: 99%

Bacterial intermediate filaments: in vivo assembly, organization, and dynamics of crescentin

Charbon

Cabeen²,

Jacobs‐Wagner³

2009

Genes Dev.

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Crescentin, which is the founding member of a rapidly growing family of bacterial cytoskeletal proteins, was previously proposed to resemble eukaryotic intermediate filament (IF) proteins based on structural prediction and in vitro polymerization properties. Here, we demonstrate that crescentin also shares in vivo properties of assembly and dynamics with IF proteins by forming stable filamentous structures that continuously incorporate subunits along their length and that grow in a nonpolar fashion. De novo assembly of crescentin is biphasic and involves a cell size-dependent mechanism that controls the length of the structure by favoring lateral insertion of crescentin subunits over bipolar longitudinal extension when the structure ends reach the cell poles. The crescentin structure is stably anchored to the cell envelope, and this cellular organization requires MreB function, identifying a new function for MreB and providing a parallel to the role of actin in IF assembly and organization in metazoan cells. Additionally, analysis of an MreB localization mutant suggests that cell wall insertion during cell elongation normally occurs along two helices of opposite handedness, each counterbalancing the other's torque.[Keywords: Crescentin; Caulobacter crescentus; intermediate filament; MreB; in vivo assembly; dynamics] Supplemental material is available at http://www.genesdev.org.

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Overview of cell shape: cytoskeletons shape bacterial cells

Cited by 27 publications

References 41 publications

Lytic enzyme discovery through multigenomic sequence analysis in Clostridium perfringens

Lytic enzyme discovery through multigenomic sequence analysis in Clostridium perfringens

RodZ, a component of the bacterial core morphogenic apparatus

Bacterial intermediate filaments: in vivo assembly, organization, and dynamics of crescentin

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