Ontology highlight
ABSTRACT:
SUBMITTER: Reichmann D
PROVIDER: S-EPMC3376891 | biostudies-literature | 2012 Mar
REPOSITORIES: biostudies-literature
Reichmann Dana D Xu Ying Y Cremers Claudia M CM Ilbert Marianne M Mittelman Roni R Fitzgerald Michael C MC Jakob Ursula U
Cell 20120301 5
The redox-regulated chaperone Hsp33 protects organisms against oxidative stress that leads to protein unfolding. Activation of Hsp33 is triggered by the oxidative unfolding of its own redox-sensor domain, making Hsp33 a member of a recently discovered class of chaperones that require partial unfolding for full chaperone activity. Here we address the long-standing question of how chaperones recognize client proteins. We show that Hsp33 uses its own intrinsically disordered regions to discriminate ...[more]