Rotate into shape: MreB and bacterial morphogenesis

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Rotate into shape: MreB and bacterial morphogenesis.

MreB, the bacterial actin homologue, plays a vital role in determining cell shape, but the mechanisms by which it actually functions have remained largely mysterious. Recent studies now shed new light on MreB, demonstrating that it associates with many cell-wall synthesis enzymes, including a newly identified family of proteins that mediate teichoic acid synthesis in Gram-positive bacteria. Fur...

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MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus.

The bacterial actin homologue, MreB, is required for the maintenance of a rod-shaped cell and has been shown to form spirals that traverse along the longitudinal axis of Bacillus subtilis and Escherichia coli cells. The depletion of MreB in Caulobacter crescentus resulted in lemon-shaped cells that possessed defects in the integrity of the cell wall. MreB localization appeared as bands or spira...

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The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes.

MreB, the bacterial actin homologue, is thought to function in spatially co-ordinating cell morphogenesis in conjunction with MreC, a protein that wraps around the outside of the cell within the periplasmic space. In Caulobacter crescentus, MreC physically associates with penicillin-binding proteins (PBPs) which catalyse the insertion of intracellularly synthesized precursors into the peptidogl...

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Direct Membrane Binding by Bacterial Actin MreB

Bacterial actin MreB is one of the key components of the bacterial cytoskeleton. It assembles into short filaments that lie just underneath the membrane and organize the cell wall synthesis machinery. Here we show that MreB from both T. maritima and E. coli binds directly to cell membranes. This function is essential for cell shape determination in E. coli and is proposed to be a general proper...

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Bacterial actin MreB forms antiparallel double filaments

Filaments of all actin-like proteins known to date are assembled from pairs of protofilaments that are arranged in a parallel fashion, generating polarity. In this study, we show that the prokaryotic actin homologue MreB forms pairs of protofilaments that adopt an antiparallel arrangement in vitro and in vivo. We provide an atomic view of antiparallel protofilaments of Caulobacter MreB as appar...

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ژورنال

عنوان ژورنال: The EMBO Journal

سال: 2011

ISSN: 0261-4189

DOI: 10.1038/emboj.2011.430