Molecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from Pseudomonas aeruginosa

Molecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from Pseudomonas aeruginosa

HtrA-family proteases are commonly employed to sense the protein folding stress and activate the regulated intramembrane proteolysis (RIP) cascade in Gram-negative bacteria. Here, we reveal the unique dual-signal activation and dynamic regulation properties of AlgW, an HtrA-type protease triggerin...

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Autores principales: Tao Li, Yingjie Song, Liming Luo, Ninglin Zhao, Lihui He, Mei Kang, Changcheng Li, Yibo Zhu, Yalin Shen, Chang Zhao, Jing Yang, Qin Huang, Xingyu Mou, Zhiyong Zong, Jinliang Yang, Hong Tang, Yongxing He, Rui Bao
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Lenguaje:EN
Publicado: American Society for Microbiology 2021
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Microbiology
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Acceso en línea:https://doaj.org/article/3d364595942a4765b601a32837d729aa
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spelling oai:doaj.org-article:3d364595942a4765b601a32837d729aa2021-11-03T18:15:37ZMolecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from Pseudomonas aeruginosa2161-21292150-751110.1128/mBio.03299-20https://doaj.org/article/3d364595942a4765b601a32837d729aa2021-02-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.03299-20https://doaj.org/toc/2161-2129https://doaj.org/toc/2150-7511 HtrA-family proteases are commonly employed to sense the protein folding stress and activate the regulated intramembrane proteolysis (RIP) cascade in Gram-negative bacteria. Here, we reveal the unique dual-signal activation and dynamic regulation properties of AlgW, an HtrA-type protease triggering the AlgU stress-response pathway, which controls alginate production and mucoid conversion in Pseudomonas aeruginosaTao LiYingjie SongLiming LuoNinglin ZhaoLihui HeMei KangChangcheng LiYibo ZhuYalin ShenChang ZhaoJing YangQin HuangXingyu MouZhiyong ZongJinliang YangHong TangYongxing HeRui BaoAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 12, Iss 1 (2021)
institution DOAJ
collection DOAJ
language EN
topic Microbiology
QR1-502
spellingShingle Microbiology
QR1-502
Tao Li
Yingjie Song
Liming Luo
Ninglin Zhao
Lihui He
Mei Kang
Changcheng Li
Yibo Zhu
Yalin Shen
Chang Zhao
Jing Yang
Qin Huang
Xingyu Mou
Zhiyong Zong
Jinliang Yang
Hong Tang
Yongxing He
Rui Bao
Molecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from Pseudomonas aeruginosa
description HtrA-family proteases are commonly employed to sense the protein folding stress and activate the regulated intramembrane proteolysis (RIP) cascade in Gram-negative bacteria. Here, we reveal the unique dual-signal activation and dynamic regulation properties of AlgW, an HtrA-type protease triggering the AlgU stress-response pathway, which controls alginate production and mucoid conversion in Pseudomonas aeruginosa
format article
author Tao Li
Yingjie Song
Liming Luo
Ninglin Zhao
Lihui He
Mei Kang
Changcheng Li
Yibo Zhu
Yalin Shen
Chang Zhao
Jing Yang
Qin Huang
Xingyu Mou
Zhiyong Zong
Jinliang Yang
Hong Tang
Yongxing He
Rui Bao
author_facet Tao Li
Yingjie Song
Liming Luo
Ninglin Zhao
Lihui He
Mei Kang
Changcheng Li
Yibo Zhu
Yalin Shen
Chang Zhao
Jing Yang
Qin Huang
Xingyu Mou
Zhiyong Zong
Jinliang Yang
Hong Tang
Yongxing He
Rui Bao
author_sort Tao Li
title Molecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from Pseudomonas aeruginosa
title_short Molecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from Pseudomonas aeruginosa
title_full Molecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from Pseudomonas aeruginosa
title_fullStr Molecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from Pseudomonas aeruginosa
title_full_unstemmed Molecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from Pseudomonas aeruginosa
title_sort molecular basis of the versatile regulatory mechanism of htra-type protease algw from pseudomonas aeruginosa
publisher American Society for Microbiology
publishDate 2021
url https://doaj.org/article/3d364595942a4765b601a32837d729aa
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