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Allosteric regulation of a prokaryotic small Ras-like GTPase contributes to cell polarity oscillations in bacterial motility

Show simple item record BARANWAL, JYOTI en_US Lhospice, Sebastien en_US KANADE, MANIL en_US CHAKRABORTY, SUKANYA en_US GADE, PRIYANKA RAJENDRA en_US HARNE, SHRIKANT en_US Herrou, Julien en_US Mignot, Tam en_US PANANGHAT, GAYATHRI en_US 2019-10-25T10:20:08Z 2019-10-25T10:20:08Z 2019-09 en_US
dc.identifier.citation PLOS Biology, 17(9). en_US
dc.identifier.issn 1544-9173 en_US
dc.identifier.uri en_US
dc.description.abstract Mutual gliding motility A (MglA), a small Ras-like GTPase; Mutual gliding motility B (MglB), its GTPase activating protein (GAP); and Required for Motility Response Regulator (RomR), a protein that contains a response regulator receiver domain, are major components of a GTPase-dependent biochemical oscillator that drives cell polarity reversals in the bacterium Myxococcus xanthus. We report the crystal structure of a complex of M. xanthus MglA and MglB, which reveals that the C-terminal helix (Ct-helix) from one protomer of the dimeric MglB binds to a pocket distal to the active site of MglA. MglB increases the GTPase activity of MglA by reorientation of key catalytic residues of MglA (a GAP function) combined with allosteric regulation of nucleotide exchange by the Ct-helix (a guanine nucleotide exchange factor [GEF] function). The dual GAP-GEF activities of MglB accelerate the rate of GTP hydrolysis over multiple enzymatic cycles. Consistent with its GAP and GEF activities, MglB interacts with MglA bound to either GTP or GDP. The regulation is essential for cell polarity, because deletion of the Ct-helix causes bipolar localization of MglA, MglB, and RomR, thereby causing reversal defects in M. xanthus. A bioinformatics analysis reveals the presence of Ct-helix in homologues of MglB in other bacterial phyla, suggestive of the prevalence of the allosteric mechanism among other prokaryotic small Ras-like GTPases. en_US
dc.language.iso en en_US
dc.publisher Public Library Science en_US
dc.subject Biology en_US
dc.subject TOC-OCT-2019 en_US
dc.subject 2019 en_US
dc.title Allosteric regulation of a prokaryotic small Ras-like GTPase contributes to cell polarity oscillations in bacterial motility en_US
dc.type Article en_US
dc.contributor.department Dept. of Biology en_US
dc.identifier.sourcetitle PLOS Biology en_US
dc.publication.originofpublisher Foreign en_US

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