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.
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Nature Portfolio
2020
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oai:doaj.org-article:e72272f032014c63830d698e467f37092021-12-02T17:01:35ZA deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi10.1038/s41467-020-15985-42041-1723https://doaj.org/article/e72272f032014c63830d698e467f37092020-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15985-4https://doaj.org/toc/2041-1723Many 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.Jason M. BerkChristopher LimJudith A. RonauApala ChaudhuriHongli ChenJohn F. BeckmannJ. Patrick LoriaYong XiongMark HochstrasserNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-17 (2020) |
| institution |
DOAJ |
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DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q 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 |
| 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. |
| format |
article |
| author |
Jason M. Berk Christopher Lim Judith A. Ronau Apala Chaudhuri Hongli Chen John F. Beckmann J. Patrick Loria Yong Xiong Mark Hochstrasser |
| 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 Portfolio |
| publishDate |
2020 |
| url |
https://doaj.org/article/e72272f032014c63830d698e467f3709 |
| work_keys_str_mv |
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| _version_ |
1718382120557084672 |