Characterization of the reovirus lambda 1 protein RNA 5'-triphosphatase activity

被引:49
作者
Bisaillon, M [1 ]
Lemay, G [1 ]
机构
[1] UNIV MONTREAL,DEPT MICROBIOL & IMMUNOL,MONTREAL,PQ H3C 3J7,CANADA
关键词
D O I
10.1074/jbc.272.47.29954
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Characterization of the phosphohydrolytic activities of recombinant reovirus lambda 1 protein demonstrates that, in addition to the previously reported nucleoside triphosphate phosphohydrolase and helicase activities, the protein also possesses RNA 5'-triphosphatase activity, This activity was absolutely dependent on the presence of a divalent cation, Mg2+ or Mn2+, and specifically removes the 5'-gamma-phosphate at the end of triphosphate-terminated RNAs, Kinetic competition analysis showed that nucleoside triphosphate phosphohydrolase and RNA 5'-triphosphatase reactions are carried out at a common active site, These results strongly support the idea that, in addition to its role as an RNA helicase during transcription of the viral genome, lambda 1 also participates during formation of the cap structure at the 5' end of newly synthesized reovirus mRNAs, The lambda 1 protein represents only the third RNA triphosphatase whose primary structure is known and the first described in a double stranded RNA virus.
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页码:29954 / 29957
页数:4
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