The α4 and α7 subunits and assembly of the 20S proteasome

被引:15
作者
Apcher, GS
Maitland, J
Dawson, S
Sheppard, P
Mayer, RJ [1 ]
机构
[1] Univ Nottingham, Sch Med, Queens Med Ctr, Lab Intracellular Proteolysis,Sch Biomed Sci, Nottingham NG7 2UH, England
[2] Biomol Int LP, Exeter EX2 8NL, Devon, England
关键词
20S proteasome; alpha-subunit; two-hybrid system; in vitro translation; alpha-ring assembly;
D O I
10.1016/j.febslet.2004.05.067
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 detailed mechanism of eukaryotic 20S proteasome assembly is currently unknown. In the present study, we demonstrate that the 20S proteasome subunits alpha4 and alpha7 interact with each other as well as all the alpha-subunits in vivo and in vitro. The N-terminal parts of alpha4 and alpha7 are essential for these newly discovered interactions in vitro. Glycerol gradient centrifugation of soluble extracts of HEK293 cells and Western blot analyses show that several a-subunits are found in non-proteasomal low-density fractions. The alpha4 and alpha7 subunits co-immunoprecipitate together from these low-density fractions. The unexpected interaction between alpha4 and alpha7 may provide a molecular basis for the formation of previously reported 13S and 16S assembly intermediates. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:211 / 216
页数:6
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