气候变化领域集成服务门户(CCPortal): An ATP-dependent partner switch links flagellar C-ring assembly with gene expression

CCPortal

DOI	10.1073/pnas.2006470117
	An ATP-dependent partner switch links flagellar C-ring assembly with gene expression
	Blagotinsek V.; Schwan M.; Steinchen W.; Mrusek D.; Hook J.C.; Rossmann F.; Freibert S.A.; Kratzat H.; Murat G.; Kressler D.; Beckmann R.; Beeby M.; Thormann K.M.; Bange G.
发表日期	2020
ISSN	0027-8424
起始页码	20826
结束页码	20835
卷号	117 期号:34
英文摘要	Bacterial flagella differ in their number and spatial arrangement. In many species, the MinD-type ATPase FlhG (also YlxH/FleN) is central to the numerical control of bacterial flagella, and its deletion in polarly flagellated bacteria typically leads to hyperflagellation. The molecular mechanism underlying this numerical control, however, remains enigmatic. Using the model species Shewanella putrefaciens, we show that FlhG links assembly of the flagellar C ring with the action of the master transcriptional regulator FlrA (named FleQ in other species). While FlrA and the flagellar C-ring protein FliM have an overlapping binding site on FlhG, their binding depends on the ATP-dependent dimerization state of FlhG. FliM interacts with FlhG independent of nucleotide binding, while FlrA exclusively interacts with the ATP-dependent FlhG dimer and stimulates FlhG ATPase activity. Our in vivo analysis of FlhG partner switching between FliM and FlrA reveals its mechanism in the numerical restriction of flagella, in which the transcriptional activity of FlrA is down-regulated through a negative feedback loop. Our study demonstrates another level of regulatory complexity underlying the spationumerical regulation of flagellar biogenesis and implies that flagellar assembly transcriptionally regulates the production of more initial building blocks. © 2020 National Academy of Sciences. All rights reserved.
英文关键词	ATPase; Flagellum; Nanomachine; Regulation; Spatiotemporal
语种	英语
scopus关键词	adenosine triphosphatase; adenosine triphosphatase FlhG; adenosine triphosphatase FliM; adenosine triphosphatase FlrA; unclassified drug; adenosine triphosphatase; adenosine triphosphate; bacterial protein; FliM protein, Bacteria; monomeric guanine nucleotide binding protein; amino terminal sequence; Article; binding site; controlled study; dimerization; down regulation; enzyme activation; enzyme activity; enzyme mechanism; flagellum; gene expression; in vivo study; negative feedback; nonhuman; phenotype; priority journal; protein assembly; protein binding; protein expression; protein protein interaction; Shewanella putrefaciens; bacterium; biochemistry; flagellum; gene expression; gene expression regulation; genetics; metabolism; Adenosine Triphosphatases; Adenosine Triphosphate; Bacteria; Bacterial Proteins; Biochemical Phenomena; Flagella; Gene Expression; Gene Expression Regulation, Bacterial; Monomeric GTP-Binding Proteins; Shewanella putrefaciens
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/160234
作者单位	Blagotinsek, V., Center for Synthetic Microbiology (SYNMIKRO), Philipps-University Marburg, Marburg, 35043, Germany, Department of Chemistry, Philipps-University Marburg, Marburg, 35043, Germany; Schwan, M., Department of Microbiology and Molecular Biology, Justus-Liebig-Universität, Giessen, 35392, Germany; Steinchen, W., Center for Synthetic Microbiology (SYNMIKRO), Philipps-University Marburg, Marburg, 35043, Germany, Department of Chemistry, Philipps-University Marburg, Marburg, 35043, Germany; Mrusek, D., Center for Synthetic Microbiology (SYNMIKRO), Philipps-University Marburg, Marburg, 35043, Germany, Department of Chemistry, Philipps-University Marburg, Marburg, 35043, Germany; Hook, J.C., Department of Microbiology and Molecular Biology, Justus-Liebig-Universität, Giessen, 35392, Germany; Rossmann, F., Department of Microbiology and Molecular Biology, Justus-Liebig-Universität, Giessen, 35392, Germany, Department of Life Sciences, Imperial College London, London, SW7 2AZ, United Kingdom; Freibert...
推荐引用方式 GB/T 7714	Blagotinsek V.,Schwan M.,Steinchen W.,et al. An ATP-dependent partner switch links flagellar C-ring assembly with gene expression[J],2020,117(34).
APA	Blagotinsek V..,Schwan M..,Steinchen W..,Mrusek D..,Hook J.C..,...&Bange G..(2020).An ATP-dependent partner switch links flagellar C-ring assembly with gene expression.Proceedings of the National Academy of Sciences of the United States of America,117(34).
MLA	Blagotinsek V.,et al."An ATP-dependent partner switch links flagellar C-ring assembly with gene expression".Proceedings of the National Academy of Sciences of the United States of America 117.34(2020).