THE SHORT-LIVED MAT-ALPHA-2 TRANSCRIPTIONAL REGULATOR IS UBIQUITINATED INVIVO

被引：230
作者：
HOCHSTRASSER, M
ELLISON, MJ
CHAU, V
VARSHAVSKY, A
机构：
[1] UNIV ALBERTA,DEPT BIOCHEM,EDMONTON T6G 2H7,ALBERTA,CANADA
[2] MIT,DEPT BIOL,CAMBRIDGE,MA 02139
[3] WAYNE STATE UNIV,SCH MED,DEPT PHARMACOL,DETROIT,MI 48201
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1991年 / 88卷 / 11期
关键词：
UBIQUITIN; PROTEIN DEGRADATION; SACCHAROMYCES-CEREVISIAE; ALPHA-2; REPRESSOR; EPITOPE TAGGING;
D O I：
10.1073/pnas.88.11.4606
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The substrates of ubiquitin-dependent proteolytic pathways include both damaged or otherwise abnormal proteins and undamaged proteins that are naturally short-lived. Few specific examples of the latter class have been identified, however. Previous work has shown that the cell type-specific MAT-alpha-2 repressor of the yeast Saccharomyces cerevisiae is an extremely short-lived protein. We now demonstrate that alpha-2 is conjugated to ubiquitin in vivo. More than one lysine residue of alpha-2 can be joined to ubiquitin, and some of the ubiquitin moieties form a Lys48-linked multiubiquitin chain. Overexpression of degradation-impaired ubiquitin variants was used to show that at least a significant fraction of alpha-2 degradation is dependent on its ubiquitination.
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页码：4606 / 4610
页数：5
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