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

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
Description
Summary: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.
ISSN:2041-1723

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