Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT

CesT is a type III secretion system chaperone that interacts with the post-transcriptional regulator CsrA, which is important for the modulation of post-attachment signaling in enteropathogenic and enterohemorrhagic Escherichia coli. Here the authors present the structure of the CsrA/CesT complex an...

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Autores principales: Fei Ye, Fanli Yang, Ruijie Yu, Xi Lin, Jianxun Qi, Zhujun Chen, Yu Cao, Yuquan Wei, George F. Gao, Guangwen Lu
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Lenguaje:EN
Publicado: Nature Portfolio 2018
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Acceso en línea:https://doaj.org/article/8f293fd685dc4dd88d5f15dce483bb3a
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spelling oai:doaj.org-article:8f293fd685dc4dd88d5f15dce483bb3a2021-12-02T17:32:16ZMolecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT10.1038/s41467-018-03625-x2041-1723https://doaj.org/article/8f293fd685dc4dd88d5f15dce483bb3a2018-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03625-xhttps://doaj.org/toc/2041-1723CesT is a type III secretion system chaperone that interacts with the post-transcriptional regulator CsrA, which is important for the modulation of post-attachment signaling in enteropathogenic and enterohemorrhagic Escherichia coli. Here the authors present the structure of the CsrA/CesT complex and propose a mechanism for CsrA-modulation by CesT.Fei YeFanli YangRuijie YuXi LinJianxun QiZhujun ChenYu CaoYuquan WeiGeorge F. GaoGuangwen LuNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Fei Ye
Fanli Yang
Ruijie Yu
Xi Lin
Jianxun Qi
Zhujun Chen
Yu Cao
Yuquan Wei
George F. Gao
Guangwen Lu
Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT
description CesT is a type III secretion system chaperone that interacts with the post-transcriptional regulator CsrA, which is important for the modulation of post-attachment signaling in enteropathogenic and enterohemorrhagic Escherichia coli. Here the authors present the structure of the CsrA/CesT complex and propose a mechanism for CsrA-modulation by CesT.
format article
author Fei Ye
Fanli Yang
Ruijie Yu
Xi Lin
Jianxun Qi
Zhujun Chen
Yu Cao
Yuquan Wei
George F. Gao
Guangwen Lu
author_facet Fei Ye
Fanli Yang
Ruijie Yu
Xi Lin
Jianxun Qi
Zhujun Chen
Yu Cao
Yuquan Wei
George F. Gao
Guangwen Lu
author_sort Fei Ye
title Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT
title_short Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT
title_full Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT
title_fullStr Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT
title_full_unstemmed Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT
title_sort molecular basis of binding between the global post-transcriptional regulator csra and the t3ss chaperone cest
publisher Nature Portfolio
publishDate 2018
url https://doaj.org/article/8f293fd685dc4dd88d5f15dce483bb3a
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