Structure and functions of arthropod proteasomes

被引:13
作者
Mykles, DL [1 ]
机构
[1] Colorado State Univ, Dept Biol, Ft Collins, CO 80523 USA
[2] Colorado State Univ, Program Mol Biol, Ft Collins, CO 80523 USA
[3] Colorado State Univ, Integrat Neurosci Program, Ft Collins, CO 80523 USA
关键词
arthropod; crustacean; Drosophila; insect; lobster; multicatalytic proteinase; proteasome; ubiquitin;
D O I
10.1023/A:1006976524916
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
Recent work on structural/functional relationships in arthropod proteasomes is reviewed. Taking advantage of our ability to induce a stable, proteolytically-active conformation of the lobster proteasome, the structures of basal and heat-activated complexes were probed with exogenous proteases. Increased sensitivity to chymotrypsin and trypsin showed that heat activation induced a more 'open' conformation, allowing entry of large substrates into the catalytic chamber. In Drosophila, the effects of two developmental mutant alleles (DTS-7 and DTS-5) encoding proteasome subunits (Z and C5, respectively) on the subunit composition and catalytic activities of the enzyme were examined. Both qualitative and quantitative differences in compositions between wild-type (+/+) and heterozygotes ( +/DTS) indicated that incorporation of mutant subunits alters post-translational modifications of the complex. Catalytic activities, however, were similar, which suggests that the developmental defect involves other proteasome properties, such as intracellular localization and/or interactions with endogenous regulators. A hypothetical model in which DTS subunits act as poison subunits is presented.
引用
收藏
页码:103 / 111
页数:9
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