期刊
ELIFE
卷 3, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.02634
关键词
MreB; elongasome; MreBCD; cell wall; cell shape
类别
资金
- Wellcome Trust [095514/Z/11/Z] Funding Source: Wellcome Trust
- Medical Research Council [MC_U105184326] Funding Source: researchfish
- Medical Research Council [U105184326, MC_U105184326] Funding Source: Medline
- Wellcome Trust [095514/Z/11/Z, 095514] Funding Source: Medline
- MRC [MC_U105184326] Funding Source: UKRI
Filaments of all actin-like proteins known to date are assembled from pairs of protofilaments that are arranged in a parallel fashion, generating polarity. Here 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 apparent from crystal structures. We show that a protofilament doublet is essential for MreB's function in cell shape maintenance and demonstrate by in vivo site-specific cross-linking the antiparallel orientation of MreB protofilaments in E. coli. 3D cryo-EM shows that pairs of protofilaments of Caulobacter MreB tightly bind to membranes. Crystal structures of different nucleotide and polymerisation states of Caulobacter MreB reveal conserved conformational changes accompanying antiparallel filament formation. Finally, the antimicrobial agents A22/MP265 are shown to bind close to the bound nucleotide of MreB, presumably preventing nucleotide hydrolysis and destabilising double protofilaments.
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