A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi

Many pathogens manipulate ubiquitin-mediated signaling to evade host cell defense. Here, the authors characterize the structure and enzymatic activity of a deubiquitylase domain from the causative pathogen of scrub typhus, providing evidence for a distinct mechanism of ubiquitin chain selectivity.

Bibliographic Details
Main Authors:	Jason M. Berk, Christopher Lim, Judith A. Ronau, Apala Chaudhuri, Hongli Chen, John F. Beckmann, J. Patrick Loria, Yong Xiong, Mark Hochstrasser
Format:	Article
Language:	English
Published:	Nature Publishing Group 2020-05-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-020-15985-4

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spelling	doaj-e72272f032014c63830d698e467f37092021-05-11T14:50:13ZengNature Publishing GroupNature Communications2041-17232020-05-0111111710.1038/s41467-020-15985-4A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushiJason M. Berk0Christopher Lim1Judith A. Ronau2Apala Chaudhuri3Hongli Chen4John F. Beckmann5J. Patrick Loria6Yong Xiong7Mark Hochstrasser8Department of Molecular Biophysics and Biochemistry, Yale UniversityDepartment of Molecular Biophysics and Biochemistry, Yale UniversityDepartment of Molecular Biophysics and Biochemistry, Yale UniversityDepartment of Chemistry, Yale UniversityDepartment of Molecular Biophysics and Biochemistry, Yale UniversityDepartment of Molecular Biophysics and Biochemistry, Yale UniversityDepartment of Molecular Biophysics and Biochemistry, Yale UniversityDepartment of Molecular Biophysics and Biochemistry, Yale UniversityDepartment of Molecular Biophysics and Biochemistry, Yale UniversityMany pathogens manipulate ubiquitin-mediated signaling to evade host cell defense. Here, the authors characterize the structure and enzymatic activity of a deubiquitylase domain from the causative pathogen of scrub typhus, providing evidence for a distinct mechanism of ubiquitin chain selectivity.https://doi.org/10.1038/s41467-020-15985-4
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Jason M. Berk Christopher Lim Judith A. Ronau Apala Chaudhuri Hongli Chen John F. Beckmann J. Patrick Loria Yong Xiong Mark Hochstrasser
spellingShingle	Jason M. Berk Christopher Lim Judith A. Ronau Apala Chaudhuri Hongli Chen John F. Beckmann J. Patrick Loria Yong Xiong Mark Hochstrasser A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi Nature Communications
author_facet	Jason M. Berk Christopher Lim Judith A. Ronau Apala Chaudhuri Hongli Chen John F. Beckmann J. Patrick Loria Yong Xiong Mark Hochstrasser
author_sort	Jason M. Berk
title	A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi
title_short	A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi
title_full	A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi
title_fullStr	A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi
title_full_unstemmed	A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi
title_sort	deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen orientia tsutsugamushi
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2020-05-01
description	Many pathogens manipulate ubiquitin-mediated signaling to evade host cell defense. Here, the authors characterize the structure and enzymatic activity of a deubiquitylase domain from the causative pathogen of scrub typhus, providing evidence for a distinct mechanism of ubiquitin chain selectivity.
url	https://doi.org/10.1038/s41467-020-15985-4
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A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi

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