INTERACTION OF TURNIP YELLOW MOSAIC-VIRUS VAL-RNA WITH EUKARYOTIC ELONGATION-FACTOR EF-1-ALPHA - SEARCH FOR A FUNCTION

被引:69
作者
JOSHI, RL
RAVEL, JM
HAENNI, AL
机构
[1] UNIV PARIS 07, F-75251 PARIS 05, FRANCE
[2] UNIV TEXAS, DEPT CHEM, AUSTIN, TX 78712 USA
[3] UNIV TEXAS, CLAYTON FDN BIOCHEM INST, AUSTIN, TX 78712 USA
关键词
D O I
10.1002/j.1460-2075.1986.tb04339.x
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
The 3''-terminal tRNA-like structure in turnip yellow mosaic virus (TYMV) RNA can be adenylated by tRNA nucleotidyltransferase and subsequently aminoacylated by valyl-tRNA synthetase. Here we present evidence that TYMV Val-RNA can form a stable complex with eukaryotic wheat germ elongation factor EF-1.alpha. and GTP: theVal-RNA is protected by EF-1.alpha. .cntdot. GTP against digestion by RNase A. By affinity chromatography of TYMV Val-RNA fragments on immobilized EF-1.alpha. .cntdot. GTP, it has been established that the valylated aminoacyl RNA domain, which in TYMV RNA is formed by the 3'' half of the tRNA-like region, is sufficient for complex formation with EF-1.alpha. .cntdot. GTP. The aminoacyl RNA domain is equivalent in tRNAs to the continuous helix formed by the acceptor stem and the T stem and loop. In line with these results, the aminoacyl RNA domain in TYMV Val-RNA complexed to EF-1.alpha. .cntdot. GTP is resistant to digestion by RNase A. It is also shown that the TYMV RNA replicase (RNA-dependent RNA polymerase) isolated from TYMV-infected Chinese cabbage leaves does not contain tRNA nucleotidyltransferase, valyl-tRNA synthetase or EF-1.alpha.. This suggests that interaction of TYMV RNA with EF-1.alpha. is not mandatory for replicase activity.
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页码:1143 / 1148
页数:6
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