Quaternary structure of the ATPase complex of human 26S proteasomes determined by chemical cross-linking

被引:57
作者
Hartmann-Petersen, R
Tanaka, K
Hendil, KB
机构
[1] Univ Copenhagen, August Krogh Inst, Dept Biochem, DK-2100 Copenhagen O, Denmark
[2] Tokyo Metropolitan Inst Med Sci, Bunkyo Ku, Tokyo 1138613, Japan
关键词
proteasome; PA700; 19S complex; cross-linking; quaternary structure;
D O I
10.1006/abbi.2000.2178
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The 26S proteasome is the major protease responsible for nonlysosomal protein degradation in eukaryotic cells. The enzyme is composed of two subparticles: the 20S proteasome, and a 19S regulatory particle (PA700) which binds to the ends of the 20S proteasome cylinder and accounts for ATP dependence and substrate specificity. Among the approximately 18 sub-units of PA700 regulator, six are ATPases, The ATPases presumably recognize, unfold, and translocate substrates into the interior of the 26S proteasome. It is generally believed that the ATPases form a hexameric ring. By means of chemical cross-linking, immunoprecipitation, and blotting, we have determined that the ATPases are organized in the order S6-S6'-S10b-S8-S4-S7. Additionally, we found cross-links between the ATPase S10b and the 20S proteasome subunit alpha6. Together with the previously known interaction between S8 and alpha1 and between S4 and alpha7, these data establish the relative orientations of ATPases with respect to the 20S proteasome. (C) 2001 Academic Press.
引用
收藏
页码:89 / 94
页数:6
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