SPECIFIC BINDING OF HOST-CELL PROTEINS TO THE 3'-TERMINAL STEM-LOOP STRUCTURE OF RUBELLA-VIRUS NEGATIVE-STRAND RNA
SPECIFIC BINDING OF HOST-CELL PROTEINS TO THE 3'-TERMINAL STEM-LOOP STRUCTURE OF RUBELLA-VIRUS NEGATIVE-STRAND RNA
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DOI:
10.1128/jvi.65.11.5961-5967.1991
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发表时间:
1991-11-01
影响因子:
5.4
通讯作者:
LIU, TY
中科院分区:
文献类型:
--
作者:
NAKHASI, HL;CAO, XQ;LIU, TY
At the 5' end of the rubella virus genomic RNA, there are sequences that can form a potentially stable stem-loop (SL) structure. The complementary negative-strand equivalent of the 5'-end SL structure of positive-strand rubella virus RNA [5' (+) SL structure] is thought to serve as a promoter for the initiation of positive-strand synthesis. We screened the negative-strand equivalent of the 5' (+) SL structure (64 nucleotides) and the adjacent region of the negative-strand RNA for their ability to bind to host cell proteins. Specific binding to the 64-nucleotide-long potential SL structure of three cytosolic proteins with relative molecular masses of 97, 79, and 56 kDa was observed by UV-induced covalent cross-linking. There was a significant increase in the binding of the 97-kDa protein from cells upon infection with rubella virus. Altering the SL structure by deleting sequences in either one of the two potential loops abolished the binding interaction. The 56-kDa protein also appeared to bind specifically to an SL derived from the 3' end of positive-strand RNA. The 3'-terminal structure of rubella virus negative-strand RNA shared the same protein-binding activity with similar structures in alphaviruses, such as Sindbis virus and eastern equine encephalitis virus. A possible role for the host proteins in the replication of rubella virus and alphaviruses is discussed.