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Slipping up: Partial substrate degradation by ATP‐dependent proteases
Author(s) -
Nassif Nicholas D.,
Cambray Samantha E.,
Kraut Daniel A.
Publication year - 2014
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.1271
Subject(s) - proteases , protease , protein degradation , degradation (telecommunications) , chemistry , biochemistry , microbiology and biotechnology , proteolysis , intracellular , biophysics , biology , enzyme , telecommunications , computer science
ATP‐dependent proteases are present in all organisms, where they are responsible for much of intracellular protein degradation. Most proteins are processively unfolded and degraded into small peptides; however, in a few so‐called slippery substrates, the protease stalls at a folded domain and releases a large protein fragment. In this review, we describe the properties of physiological slippery substrates that are processed in this manner by ATP‐dependent proteases and the recent advances that have been made in understanding the mechanism underlying their partial degradation. © 2014 IUBMB Life, 66(5):309–317, 2014