Ontology highlight
ABSTRACT:
SUBMITTER: Shi Y
PROVIDER: S-EPMC4980823 | biostudies-literature | 2016 Feb
REPOSITORIES: biostudies-literature
Shi Yuan Y Chen Xiang X Elsasser Suzanne S Stocks Bradley B BB Tian Geng G Lee Byung-Hoon BH Shi Yanhong Y Zhang Naixia N de Poot Stefanie A H SA Tuebing Fabian F Sun Shuangwu S Vannoy Jacob J Tarasov Sergey G SG Engen John R JR Finley Daniel D Walters Kylie J KJ
Science (New York, N.Y.) 20160201 6275
Hundreds of pathways for degradation converge at ubiquitin recognition by a proteasome. Here, we found that the five known proteasomal ubiquitin receptors in yeast are collectively nonessential for ubiquitin recognition and identified a sixth receptor, Rpn1. A site ( T1: ) in the Rpn1 toroid recognized ubiquitin and ubiquitin-like ( UBL: ) domains of substrate shuttling factors. T1 structures with monoubiquitin or lysine 48 diubiquitin show three neighboring outer helices engaging two ubiquitins ...[more]