a response regulator interfaces between the frz chemosensory system and the mglamglb gtpasegap module to regulate polarity in myxococcus xanthus响应监管机构之间的接口frz化学感应的系统和mglamglb gtpasegap模块来调节极性在myxococcus克桑托斯.pdfVIP

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a response regulator interfaces between the frz chemosensory system and the mglamglb gtpasegap module to regulate polarity in myxococcus xanthus响应监管机构之间的接口frz化学感应的系统和mglamglb gtpasegap模块来调节极性在myxococcus克桑托斯.pdf

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a response regulator interfaces between the frz chemosensory system and the mglamglb gtpasegap module to regulate polarity in myxococcus xanthus响应监管机构之间的接口frz化学感应的系统和mglamglb gtpasegap模块来调节极性在myxococcus克桑托斯

A Response Regulator Interfaces between the Frz Chemosensory System and the MglA/MglB GTPase/GAP Module to Regulate Polarity in Myxococcus xanthus Daniela Keilberg, Kristin Wuichet, Florian Drescher, Lotte Søgaard-Andersen* Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany Abstract How cells establish and dynamically change polarity are general questions in cell biology. Cells of the rod-shaped bacterium Myxococcus xanthus move on surfaces with defined leading and lagging cell poles. Occasionally, cells undergo reversals, which correspond to an inversion of the leading-lagging pole polarity axis. Reversals are induced by the Frz chemosensory system and depend on relocalization of motility proteins between the poles. The Ras-like GTPase MglA localizes to and defines the leading cell pole in the GTP-bound form. MglB, the cognate MglA GTPase activating protein, localizes to and defines the lagging pole. During reversals, MglA-GTP and MglB switch poles and, therefore, dynamically localized motility proteins switch poles. We identified the RomR response regulator, which localizes in a bipolar asymmetric pattern with a large cluster at the lagging pole, as important for motility and reversals. We show that RomR interacts directly with MglA and MglB in vitro. Furthermore, RomR, MglA, and MglB affect the localization of each other in all pair-wise directions, suggesting that RomR stimulates motility by promoting correct localization of MglA and MglB in MglA/RomR and MglB/ RomR complexes at opposite poles. Moreover, localization analyses suggest that the two RomR complexes mutually exclude each other from their respective poles. We further show that RomR interfaces with FrzZ, the output response regulator of the Frz chemosensory system, to regulate reversals. Thus, RomR serves at the functional