共查询到20条相似文献,搜索用时 31 毫秒
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Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product 总被引:45,自引:0,他引:45
D Defeo-Jones P S Huang R E Jones K M Haskell G A Vuocolo M G Hanobik H E Huber A Oliff 《Nature》1991,352(6332):251-254
The E7 transforming protein of human papilloma virus-16 binds to the retinoblastoma gene product (pRb) through a nine-amino-acid segment of E7 (21-29). This segment of E7 is homologous to the pRb-binding domains of the simian virus 40 large T and adenovirus E1A transforming proteins. Each of these viral transforming proteins bind to the same region of pRb. To isolate cellular proteins that interact with this viral protein-binding domain on pRb, we used recombinant pRb to screen a human complementary DNA expression library. Two cDNAs were isolated that encode retinoblastoma binding proteins (RBP-1 and RBP-2). We report here that these RBP genes exist in separate loci and produce discrete messenger RNAs. The predicted amino-acid sequence of these genes showed no homology to known proteins, but both RBPs contain the pRb binding motif conserved between E7, large T and E1A14. In vitro expression of the RBP cDNAs yielded proteins that specifically bound to pRb. Recombinant E7 protein, the E7 21-29 peptide and the homologous RBP-1 peptide inhibited RBP-pRb binding. Mutations introduced into the putative pRb-binding segment in RBP-1 impaired its binding activity. These studies indicate that the cellular RBP-1, RBP-2 and viral E7 proteins interact with pRb through similar domains. 相似文献
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Architecture of the Mediator head module 总被引:1,自引:0,他引:1
Imasaki T Calero G Cai G Tsai KL Yamada K Cardelli F Erdjument-Bromage H Tempst P Berger I Kornberg GL Asturias FJ Kornberg RD Takagi Y 《Nature》2011,475(7355):240-243
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