Ontology highlight
ABSTRACT:
SUBMITTER: Bashore C
PROVIDER: S-EPMC4560640 | biostudies-literature | 2015 Sep
REPOSITORIES: biostudies-literature
Bashore Charlene C Dambacher Corey M CM Goodall Ellen A EA Matyskiela Mary E ME Lander Gabriel C GC Martin Andreas A
Nature structural & molecular biology 20150824 9
Substrates are targeted for proteasomal degradation through the attachment of ubiquitin chains that need to be removed by proteasomal deubiquitinases before substrate processing. In budding yeast, the deubiquitinase Ubp6 trims ubiquitin chains and affects substrate processing by the proteasome, but the underlying mechanisms and the location of Ubp6 within the holoenzyme have been elusive. Here we show that Ubp6 activity strongly responds to interactions with the base ATPase and the conformationa ...[more]