Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome

被引:122
作者
vanNocker, S
Deveraux, Q
Rechsteiner, M
Vierstra, RD
机构
[1] UNIV WISCONSIN,DEPT HORT,MADISON,WI 53706
[2] UNIV UTAH,SCH MED,DEPT BIOCHEM,SALT LAKE CITY,UT 84132
关键词
protein degradation; proteolysis inhibitor; protein interaction; human;
D O I
10.1073/pnas.93.2.856
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
Multiubiquitin chain attachment is a key step leading to the selective degradation of abnormal polypeptides and many important regulatory proteins by the eukaryotic 26S proteasome. However, the mechanism by which the 26S complex recognizes this posttranslational modification is unknown, Using synthetic multiubiquitin chains to probe an expression library for interacting proteins, we have isolated an Arabidopsis cDNA, designated MBP1, that encodes a 41-kDa acidic protein exhibiting high affinity for chains, especially those containing four or more ubiquitins. Based on similar physical and immunological properties, multiubiquitin binding affinities, and peptide sequence, MBP1 is homologous to subunit 5a of the human 26S proteasome. Structurally related proteins also exist in yeast, Caenorhabditis, and other plant species, Given their binding properties, association with the 26S proteasome, and widespread distribution, MBP1, S5a, and related proteins likely function as essential ubiquitin recognition components of the 26S proteasome.
引用
收藏
页码:856 / 860
页数:5
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