气候变化领域集成服务门户(CCPortal): The small GTPase MglA together with the TPR domain protein SgmX stimulates type IV pili formation in M. xanthus

CCPortal

DOI	10.1073/pnas.2004722117
	The small GTPase MglA together with the TPR domain protein SgmX stimulates type IV pili formation in M. xanthus
	Potapova A.; Carreira L.A.M.; Søgaard-Andersen L.
发表日期	2020
ISSN	0027-8424
起始页码	23859
结束页码	23868
卷号	117 期号:38
英文摘要	Bacteria can move across surfaces using type IV pili (T4P), which undergo cycles of extension, adhesion, and retraction. The T4P localization pattern varies between species; however, the underlying mechanisms are largely unknown. In the rod-shaped Myxococcus xanthus cells, T4P localize at the leading cell pole. As cells reverse their direction of movement, T4P are disassembled at the old leading pole and then form at the new leading pole. Thus, cells can form T4P at both poles but engage only one pole at a time in T4P formation. Here, we address how this T4P unipolarity is realized. We demonstrate that the small Ras-like GTPase MglA stimulates T4P formation in its GTP-bound state by direct interaction with the tetratricopeptide repeat (TPR) domain-containing protein SgmX. SgmX, in turn, is important for polar localization of the T4P extension ATPase PilB. The cognate MglA GTPase activating protein (GAP) MglB, which localizes mainly to the lagging cell pole, indirectly blocks T4P formation at this pole by stimulating the conversion of MglA-GTP to MglA-GDP. Based on these findings, we propose a model whereby T4P unipolarity is accomplished by stimulation of T4P formation at the leading pole by MglA-GTP and SgmX and indirect inhibition of T4P formation at the lagging pole by MglB due to its MglA GAP activity. During reversals, MglA, SgmX, and MglB switch polarity, thus laying the foundation for T4P formation at the new leading pole and inhibition of T4P formation at the new lagging pole. © 2020 National Academy of Sciences. All rights reserved.
英文关键词	Bacterial motility; bacterial polarity; MglA GTPase; PilB ATPase; type IV pili
语种	英语
scopus关键词	guanosine triphosphatase; guanosine triphosphatase MglA; protein SgmX; tetratricopeptide repeat protein; unclassified drug; bacterial protein; fimbria protein; MglA protein, Myxococcus xanthus; Article; bacterial cell; bacterial strain; bacterium pilus; cell motility; cell polarity; controlled study; enzyme inhibition; genotype; Myxococcus xanthus; nonhuman; priority journal; protein function; protein localization; type IV secretion system; chemistry; fimbria; genetics; metabolism; tetratricopeptide repeat; Bacterial Proteins; Cell Polarity; Fimbriae Proteins; Fimbriae, Bacterial; Tetratricopeptide Repeat
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160219
作者单位	Potapova, A., Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, 35043, Germany; Carreira, L.A.M., Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, 35043, Germany; Søgaard-Andersen, L., Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Marburg, 35043, Germany
推荐引用方式 GB/T 7714	Potapova A.,Carreira L.A.M.,Søgaard-Andersen L.. The small GTPase MglA together with the TPR domain protein SgmX stimulates type IV pili formation in M. xanthus[J],2020,117(38).
APA	Potapova A.,Carreira L.A.M.,&Søgaard-Andersen L..(2020).The small GTPase MglA together with the TPR domain protein SgmX stimulates type IV pili formation in M. xanthus.Proceedings of the National Academy of Sciences of the United States of America,117(38).
MLA	Potapova A.,et al."The small GTPase MglA together with the TPR domain protein SgmX stimulates type IV pili formation in M. xanthus".Proceedings of the National Academy of Sciences of the United States of America 117.38(2020).