Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex

ClpXP is the main ATP-dependent proteolytic complex in bacteria, is essential for maintaining cellular protein homeostasis and is also critical for bacterial pathogenesis. Here, the authors establish a functional link between ClpXP and trigger actor, a chaperone involved in the early stages of prote...

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Autores principales: Kamran Rizzolo, Angela Yeou Hsiung Yu, Adedeji Ologbenla, Sa-Rang Kim, Haojie Zhu, Koichiro Ishimori, Guillaume Thibault, Elisa Leung, Yi Wen Zhang, Mona Teng, Marta Haniszewski, Noha Miah, Sadhna Phanse, Zoran Minic, Sukyeong Lee, Julio Diaz Caballero, Mohan Babu, Francis T. F. Tsai, Tomohide Saio, Walid A. Houry
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/bb669bad02bc48fc84564ad981954599
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spelling oai:doaj.org-article:bb669bad02bc48fc84564ad9819545992021-12-02T15:22:39ZFunctional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex10.1038/s41467-020-20553-x2041-1723https://doaj.org/article/bb669bad02bc48fc84564ad9819545992021-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20553-xhttps://doaj.org/toc/2041-1723ClpXP is the main ATP-dependent proteolytic complex in bacteria, is essential for maintaining cellular protein homeostasis and is also critical for bacterial pathogenesis. Here, the authors establish a functional link between ClpXP and trigger actor, a chaperone involved in the early stages of protein folding.Kamran RizzoloAngela Yeou Hsiung YuAdedeji OlogbenlaSa-Rang KimHaojie ZhuKoichiro IshimoriGuillaume ThibaultElisa LeungYi Wen ZhangMona TengMarta HaniszewskiNoha MiahSadhna PhanseZoran MinicSukyeong LeeJulio Diaz CaballeroMohan BabuFrancis T. F. TsaiTomohide SaioWalid A. HouryNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Kamran Rizzolo
Angela Yeou Hsiung Yu
Adedeji Ologbenla
Sa-Rang Kim
Haojie Zhu
Koichiro Ishimori
Guillaume Thibault
Elisa Leung
Yi Wen Zhang
Mona Teng
Marta Haniszewski
Noha Miah
Sadhna Phanse
Zoran Minic
Sukyeong Lee
Julio Diaz Caballero
Mohan Babu
Francis T. F. Tsai
Tomohide Saio
Walid A. Houry
Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex
description ClpXP is the main ATP-dependent proteolytic complex in bacteria, is essential for maintaining cellular protein homeostasis and is also critical for bacterial pathogenesis. Here, the authors establish a functional link between ClpXP and trigger actor, a chaperone involved in the early stages of protein folding.
format article
author Kamran Rizzolo
Angela Yeou Hsiung Yu
Adedeji Ologbenla
Sa-Rang Kim
Haojie Zhu
Koichiro Ishimori
Guillaume Thibault
Elisa Leung
Yi Wen Zhang
Mona Teng
Marta Haniszewski
Noha Miah
Sadhna Phanse
Zoran Minic
Sukyeong Lee
Julio Diaz Caballero
Mohan Babu
Francis T. F. Tsai
Tomohide Saio
Walid A. Houry
author_facet Kamran Rizzolo
Angela Yeou Hsiung Yu
Adedeji Ologbenla
Sa-Rang Kim
Haojie Zhu
Koichiro Ishimori
Guillaume Thibault
Elisa Leung
Yi Wen Zhang
Mona Teng
Marta Haniszewski
Noha Miah
Sadhna Phanse
Zoran Minic
Sukyeong Lee
Julio Diaz Caballero
Mohan Babu
Francis T. F. Tsai
Tomohide Saio
Walid A. Houry
author_sort Kamran Rizzolo
title Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex
title_short Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex
title_full Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex
title_fullStr Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex
title_full_unstemmed Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex
title_sort functional cooperativity between the trigger factor chaperone and the clpxp proteolytic complex
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/bb669bad02bc48fc84564ad981954599
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