Journal
EMBO JOURNAL
Volume 29, Issue 2, Pages 315-326Publisher
WILEY
DOI: 10.1038/emboj.2009.356
Keywords
A22; adhesion complexes; cell polarity; motility clusters; protein localization
Categories
Funding
- Ministere de la Recherche
- AFSSET
- National Institutes of Health [GM20509]
- ANR 'Jeunes Chercheurs-Jeunes Chercheuses' [ANR-07-JCJC-0131]
- Agence Nationale de la Recherche (ANR) [ANR-07-JCJC-0131] Funding Source: Agence Nationale de la Recherche (ANR)
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Gliding motility in the bacterium Myxococcus xanthus uses two motility engines: S-motility powered by type-IV pili and A-motility powered by uncharacterized motor proteins and focal adhesion complexes. In this paper, we identified MreB, an actin-like protein, and MglA, a small GTPase of the Ras superfamily, as essential for both motility systems. A22, an inhibitor of MreB cytoskeleton assembly, reversibly inhibited S- and A-motility, causing rapid dispersal of S- and A-motility protein clusters, FrzS and AglZ. This suggests that the MreB cytoskeleton is involved in directing the positioning of these proteins. We also found that a Delta mglA motility mutant showed defective localization of AglZ and FrzS clusters. Interestingly, MglA-YFP localization mimicked both FrzS and AglZ patterns and was perturbed by A22 treatment, consistent with results indicating that both MglA and MreB bind to motility complexes. We propose that MglA and the MreB cytoskeleton act together in a pathway to localize motility proteins such as AglZ and FrzS to assemble the A-motility machineries. Interestingly, M. xanthus motility systems, like eukaryotic systems, use an actin-like protein and a small GTPase spatial regulator. The EMBO Journal (2010) 29, 315-326. doi: 10.1038/emboj.2009.356; Published online 3 December 2009
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