Crystal structure of yeast Gid10 in complex with Pro/N-degron
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Shin, Jin Seok | - |
dc.contributor.author | Park, Si Hoon | - |
dc.contributor.author | Kim, Leehyeon | - |
dc.contributor.author | Heo, Jiwon | - |
dc.contributor.author | Song, Hyun Kyu | - |
dc.date.accessioned | 2022-02-12T05:40:47Z | - |
dc.date.available | 2022-02-12T05:40:47Z | - |
dc.date.created | 2022-02-09 | - |
dc.date.issued | 2021-12-10 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/135436 | - |
dc.description.abstract | The cellular glucose level has to be tightly regulated by a variety of cellular processes. One of them is the degradation of gluconeogenic enzymes such as Fbp1, Icl1, Mdh2, and Pck1 by GID (glucose-induced degradation deficient) E3 ubiquitin ligase. The Gid4 component of the GID ligase complex is responsible for recognizing the N-terminal proline residue of the target substrates under normal conditions. How-ever, an alternative N-recognin Gid10 controls the degradation process under stressed conditions. Although Gid10 shares a high sequence similarity with Gid4, their substrate specificities are quite different. Here, we report the structure of Gid10 from Saccharomyces cerevisiae in complex with Pro/N-degron, Pro-Tyr-Ile-Thr, which is almost identical to the sequence of the natural substrate Art2. Although Gid10 shares many structural features with the Gid4 protein from yeast and humans, the current structure explains the unique structural difference for the preference of bulky hydrophobic residue at the second position of Pro/N-degron. Therefore, this study provides a fundamental basis for understanding of the structural diversity and substrate specificity of recognition components in the GID E3 ligase complex involved in the Pro/N-degron pathway. (c) 2021 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | UBIQUITIN SYSTEM | - |
dc.subject | CATABOLITE INACTIVATION | - |
dc.subject | N-DEGRON | - |
dc.subject | DEGRADATION | - |
dc.subject | FRUCTOSE-1,6-BISPHOSPHATASE | - |
dc.subject | PROTEINS | - |
dc.subject | RECOGNITION | - |
dc.title | Crystal structure of yeast Gid10 in complex with Pro/N-degron | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Song, Hyun Kyu | - |
dc.identifier.doi | 10.1016/j.bbrc.2021.10.007 | - |
dc.identifier.scopusid | 2-s2.0-85117749736 | - |
dc.identifier.wosid | 000711418700013 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.582, pp.86 - 92 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 582 | - |
dc.citation.startPage | 86 | - |
dc.citation.endPage | 92 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | CATABOLITE INACTIVATION | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | FRUCTOSE-1,6-BISPHOSPHATASE | - |
dc.subject.keywordPlus | N-DEGRON | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | UBIQUITIN SYSTEM | - |
dc.subject.keywordAuthor | E3 ubiquitin ligase | - |
dc.subject.keywordAuthor | GID complex | - |
dc.subject.keywordAuthor | N-degron | - |
dc.subject.keywordAuthor | Proline | - |
dc.subject.keywordAuthor | Saccharomyces cerevisiae | - |
dc.subject.keywordAuthor | X-ray crystallography | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
145 Anam-ro, Seongbuk-gu, Seoul, 02841, Korea+82-2-3290-2963
COPYRIGHT © 2021 Korea University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.