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-Structure paper
タイトル | An ATP-dependent partner switch links flagellar C-ring assembly with gene expression. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 117, Issue 34, Page 20826-20835, Year 2020 |
掲載日 | 2020年8月25日 |
![]() | Vitan Blagotinsek / Meike Schwan / Wieland Steinchen / Devid Mrusek / John C Hook / Florian Rossmann / Sven A Freibert / Hanna Kratzat / Guillaume Murat / Dieter Kressler / Roland Beckmann / Morgan Beeby / Kai M Thormann / Gert Bange / ![]() ![]() ![]() |
PubMed 要旨 | 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 ...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 , 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. |
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手法 | EM (サブトモグラム平均) |
解像度 | 79.0 - 82.0 Å |
構造データ | ![]() EMDB-11059: ![]() EMDB-11060: |
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