A 26-S PROTEASE SUBUNIT THAT BINDS UBIQUITIN CONJUGATES

Citation
Q. Deveraux et al., A 26-S PROTEASE SUBUNIT THAT BINDS UBIQUITIN CONJUGATES, The Journal of biological chemistry, 269(10), 1994, pp. 7059-7061
Citations number
24
Categorie Soggetti
Biology
ISSN journal
00219258
Volume
269
Issue
10
Year of publication
1994
Pages
7059 - 7061
Database
ISI
SICI code
0021-9258(1994)269:10<7059:A2PSTB>2.0.ZU;2-5
Abstract
Ubiquitin-mediated proteolysis provides an important mechanism for reg ulating a variety of cellular processes. Ubiquitin-conjugated proteins are degraded by a 26 S protease that contains more than 30 different subunits. Of these, a single 50-kDa polypeptide, subunit 5, specifical ly binds ubiquitin-lysozyme conjugates. Binding is inhibited by short polymeric chains of ubiquitin but not by ubiquitin monomers or by lyso zyme. In addition, subunit 5 binds free ubiquitin chains with efficien t association requiring at least four ubiquitins. Thus, proteins conju gated to polymers of ubiquitin may be selected for degradation by a si ngle subunit of the 26 S protease complex.