期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 100, 期 15, 页码 8963-8968出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1533420100
关键词
ubiquitin ligase; infected cell protein 0; ring finger
资金
- NCI NIH HHS [CA88860, R37 CA078766, R01 CA083939, CA78766, P01 CA071933, P01 CA087661, CA87661, R01 CA088860, CA71933, R01 CA078766, CA83939] Funding Source: Medline
infected cell protein 0 (ICPO) of herpes simplex virus 1 expresses two E3 ubiquitin (Ub) ligase activities mapping in the domains encoded by exons 2 and 3, respectively. Site 1 (exon 3) is responsible for the degradation of the E2 Ub-conjugating enzyme cdc34 whereas site2(exon 2) is associated with a ring finger and has been shown to mediate the degradation of promyelocytic leukemia (PML) and Sp 100 proteins and the dispersal of nuclear domain 10 (ND10). In in vitro assays site 2 polyubiquitylates the E2 enzymes UbcH5a and UbcH6 but not other (e.g., UbcH7) enzymes. In this article, we show that ectopic expression of dominant negative UbcH5a carrying the substitution C85A delayed or blocked the degradation of PML and Sp 100 and dispersal of ND10 whereas ectopic expression of wild-type UbcH5a or dominant negative UbcH6 and UbcH7 carrying the substitutions C131A and C86A, respectively, had no effect. These results link the degradation of PML and Sp 100 and the dispersal of ND10 to the E3 activities of ICPO associated with the UbcH5a E2 enzyme.
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