期刊
EMBO JOURNAL
卷 29, 期 14, 页码 2276-2289出版社
WILEY
DOI: 10.1038/emboj.2010.114
关键词
cell polarity; dynamic protein localization; GTPase-activating protein; Ras-like GTPase; type IV pili
资金
- Max Planck Society
- German Research Foundation
- LOEWE Research Center for Synthetic Microbiology
The rod-shaped cells of the bacterium Myxococcus xanthus move uni-directionally and occasionally undergo reversals during which the leading/lagging polarity axis is inverted. Cellular reversals depend on pole-to-pole relocation of motility proteins that localize to the cell poles between reversals. We show that MglA is a Ras-like G-protein and acts as a nucleotide-dependent molecular switch to regulate motility and that MglB represents a novel GTPase-activating protein (GAP) family and is the cognate GAP of MglA. Between reversals, MglA/GTP is restricted to the leading and MglB to the lagging pole defining the leading/lagging polarity axis. For reversals, the Frz chemosensory system induces the relocation of MglA/GTP to the lagging pole causing an inversion of the leading/lagging polarity axis. MglA/GTP stimulates motility by establishing correct polarity of motility proteins between reversals and reversals by inducing their pole-to-pole relocation. Thus, the function of Ras-like G-proteins and their GAPs in regulating cell polarity is found not only in eukaryotes, but also conserved in bacteria. The EMBO Journal (2010) 29, 2276-2289. doi:10.1038/emboj.2010.114; Published online 11 June 2010
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