铜绿假单胞菌的外切酶S将中间丝蛋白波形蛋白进行ADP核糖基化修饰。
Exoenzyme S of Pseudomonas aeruginosa ADP-ribosylates the intermediate filament protein vimentin.
作者信息
Coburn J, Dillon S T, Iglewski B H, Gill D M
机构信息
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts.
出版信息
Infect Immun. 1989 Mar;57(3):996-8. doi: 10.1128/iai.57.3.996-998.1989.
Abstract
Exoenzyme S, which had been thought to be unselective, catalyzes the ADP-ribosylation of only a subset of cellular proteins. The intermediate filament protein vimentin is one of the more abundant substrates. Disassembled vimentin, and proteolytic fragments of vimentin that cannot form filaments, is more readily ADP-ribosylated than is filamentous vimentin.
摘要
外切酶S曾被认为没有选择性，但它仅催化细胞内一部分蛋白质的ADP核糖基化反应。中间丝蛋白波形蛋白是较丰富的底物之一。已解聚的波形蛋白以及不能形成细丝的波形蛋白蛋白水解片段，比丝状波形蛋白更容易被ADP核糖基化。
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