Association of L Protein and in vitro Tomato Spotted Wilt Virus RNA-Dependent RNA Polymerase Activity

Intervirology ◽  
2003 ◽  
Vol 46 (3) ◽  
pp. 177-181 ◽  
Author(s):  
Elisabeth J. Chapman ◽  
Pierre Hilson ◽  
Thomas L. German
1986 ◽  
Vol 6 (2) ◽  
pp. 404-410 ◽  
Author(s):  
T Fujimura ◽  
R B Wickner

pet18 mutations in Saccharomyces cerevisiae confer on the cell the inability to maintain either L-A or M double-stranded RNAs (dsRNAs) at the nonpermissive temperature. In in vitro experiments, we examined the effects of pet18 mutations on the RNA-dependent RNA polymerase activity associated with virus-like particles (VLPs). pet18 mutations caused thermolabile RNA polymerase activity of L-A VLPs, and this thermolability was found to be due to the instability of the L-A VLP structure. The pet18 mutations did not affect RNA polymerase activity of M VLPs. Furthermore, the temperature sensitivity of wild-type L-A RNA polymerase differed substantially from that of M RNA polymerase. From these results, and from other genetic and biochemical lines of evidence which suggest that replication of M dsRNA requires the presence of L-A dsRNA, we propose that the primary effect of the pet18 mutation is on the L-A VLP structure and that the inability of pet18 mutants to maintain M dsRNA comes from the loss of L-A dsRNA.


2003 ◽  
Vol 113 (1) ◽  
pp. 65-68 ◽  
Author(s):  
Douglas J DeMarini ◽  
Victor K Johnston ◽  
Madhavi Konduri ◽  
Lester L Gutshall ◽  
Robert T Sarisky

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