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| A 26-S PROTEASE SUBUNIT THAT BINDS UBIQUITIN CONJUGATES |
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| Author(s): DEVERAUX Q, USTRELL V, PICKART C, RECHSTEINER M |
| Source: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 269 Issue: 10 Pages: 7059-7061 Published: MAR 11 1994 |
| Times Cited: 392 References: 24 |
| Abstract: Ubiquitin-mediated proteolysis provides an important mechanism for regulating 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, specifically binds ubiquitin-lysozyme conjugates. Binding is inhibited by short polymeric chains of ubiquitin but not by ubiquitin monomers or by lysozyme. In addition, subunit 5 binds free ubiquitin chains with efficient association requiring at least four ubiquitins. Thus, proteins conjugated to polymers of ubiquitin may be selected for degradation by a single subunit of the 26 S protease complex. |
| Document Type: Note |
| Language: English |
| Reprint Address: DEVERAUX, Q (reprint author), UNIV UTAH, SCH MED, DEPT BIOCHEM, SALT LAKE CITY, UT 84132 USA |
Addresses:
1. SUNY BUFFALO, DEPT BIOCHEM, BUFFALO, NY 14214 USA |
| Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: NA032 |
| ISSN: 0021-9258 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |