globalchange  > 气候变化与战略
DOI: 10.1073/pnas.2006470117
论文题名:
An ATP-dependent partner switch links flagellar C-ring assembly with gene expression
作者: 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.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2020
卷: 117, 期:34
起始页码: 20826
结束页码: 20835
语种: 英语
英文关键词: ATPase ; Flagellum ; Nanomachine ; Regulation ; Spatiotemporal
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
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.
Citation statistics:
资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163406
Appears in Collections:气候变化与战略

Files in This Item:

There are no files associated with this item.


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, S.A., Institut für Zytobiologie und Zytopathologie, Philipps-Universitat Marburg, Marburg, 35032, Germany; Kratzat, H., Genzentrum, Ludwig-Maximilians-Universität, Munich, 81377, Germany, Department of Biochemistry, Ludwig-Maximilians-Universität, Munich, 81377, Germany; Murat, G., Department of Biology, University of Fribourg, Fribourg, 1700, Switzerland; Kressler, D., Department of Biology, University of Fribourg, Fribourg, 1700, Switzerland; Beckmann, R., Genzentrum, Ludwig-Maximilians-Universität, Munich, 81377, Germany, Department of Biochemistry, Ludwig-Maximilians-Universität, Munich, 81377, Germany; Beeby, M., Department of Life Sciences, Imperial College London, London, SW7 2AZ, United Kingdom; Thormann, K.M., Department of Microbiology and Molecular Biology, Justus-Liebig-Universität, Giessen, 35392, Germany; Bange, G., Center for Synthetic Microbiology (SYNMIKRO), Philipps-University Marburg, Marburg, 35043, Germany, Department of Chemistry, Philipps-University Marburg, Marburg, 35043, Germany

Recommended Citation:
Blagotinsek V.,Schwan M.,Steinchen W.,et al. An ATP-dependent partner switch links flagellar C-ring assembly with gene expression[J]. Proceedings of the National Academy of Sciences of the United States of America,2020-01-01,117(34)
Service
Recommend this item
Sava as my favorate item
Show this item's statistics
Export Endnote File
Google Scholar
Similar articles in Google Scholar
[Blagotinsek V.]'s Articles
[Schwan M.]'s Articles
[Steinchen W.]'s Articles
百度学术
Similar articles in Baidu Scholar
[Blagotinsek V.]'s Articles
[Schwan M.]'s Articles
[Steinchen W.]'s Articles
CSDL cross search
Similar articles in CSDL Cross Search
[Blagotinsek V.]‘s Articles
[Schwan M.]‘s Articles
[Steinchen W.]‘s Articles
Related Copyright Policies
Null
收藏/分享
所有评论 (0)
暂无评论
 

Items in IR are protected by copyright, with all rights reserved, unless otherwise indicated.