GENETIC-EVIDENCE THAT THE TAT PROTEINS OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 AND TYPE-2 CAN MULTIMERIZE IN THE EUKARYOTIC CELL-NUCLEUS

被引:55
作者
BOGERD, HP
FRIDELL, RA
BLAIR, WS
CULLEN, BR
机构
[1] DUKE UNIV,MED CTR,HOWARD HUGHES MED INST,DURHAM,NC 27710
[2] DUKE UNIV,MED CTR,GENET SECT,DURHAM,NC 27710
[3] DUKE UNIV,MED CTR,DEPT MICROBIOL,DURHAM,NC 27710
关键词
D O I
10.1128/JVI.67.8.5030-5034.1993
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The formation of dimers or higher-order multimers is critical to the biological activity of many eukaryotic regulatory proteins. However, biochemical analyses of the multimerization capacity of the Tat trans activator of human immunodeficiency virus types 1 (HIV-1) and 2 (HIV-2) have yielded contradictory results. We used the two-hybrid genetic assay for protein-protein interactions in the eukaryote Saccharomyces cerevisiae (S. Fields and O.-K. Song, Nature [London] 340:245-246, 1989) to examine the multimerization of Tat in vivo. Both HIV-1 and HIV-2 Tat are shown to form specific homo- but not heteromultimers in the yeast cell nucleus. Mutational analysis indicates a critical role for the essential core motif of Tat in mediating this interaction but demonstrates that efficient Tat multimerization does not require an intact cysteine motif. These data raise the possibility that the multimerization of Tat may be important for Tat function in higher eukaryotes.
引用
收藏
页码:5030 / 5034
页数:5
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