Translation of satellite tobacco necrosis virus ribonucleic acid by an in vitro system from wheat germ

Biochemistry ◽  
1976 ◽  
Vol 15 (22) ◽  
pp. 4943-4950 ◽  
Author(s):  
David W. Leung ◽  
Carl W. Gilbert ◽  
Robert E. Smith ◽  
Nancy L. Sasavage ◽  
John M. Clark
Biochemistry ◽  
1972 ◽  
Vol 11 (11) ◽  
pp. 2014-2019 ◽  
Author(s):  
Ronald E. Lundquist ◽  
Jerome M. Lazar ◽  
William H. Klein ◽  
John M. Clark

Biochemistry ◽  
1972 ◽  
Vol 11 (11) ◽  
pp. 2009-2014 ◽  
Author(s):  
William H. Klein ◽  
Chris Nolan ◽  
Jerome M. Lazar ◽  
John M. Clark

Biochemistry ◽  
1980 ◽  
Vol 19 (10) ◽  
pp. 2276-2283 ◽  
Author(s):  
Karen S. Browning ◽  
David W. Leung ◽  
John M. Clark

1979 ◽  
Vol 254 (17) ◽  
pp. 8245-8249
Author(s):  
D. Herson ◽  
A. Schmidt ◽  
S. Seal ◽  
A. Marcus ◽  
L. van Vloten-Doting

1993 ◽  
Vol 13 (6) ◽  
pp. 3340-3349 ◽  
Author(s):  
X Danthinne ◽  
J Seurinck ◽  
F Meulewaeter ◽  
M Van Montagu ◽  
M Cornelissen

The RNA of satellite tobacco necrosis virus (STNV) is a monocistronic messenger that lacks both a 5' cap structure and a 3' poly(A) tail. We show that in a cell-free translation system derived from wheat germ, STNV RNA lacking the 600-nucleotide trailer is translated an order of magnitude less efficiently than full-size RNA. Deletion analyses positioned the translational enhancer domain (TED) within a conserved hairpin structure immediately downstream from the coat protein cistron. TED enhances translation when fused to a heterologous mRNA, but the level of enhancement depends on the nature of the 5' untranslated sequence and is maximal in combination with the STNV leader. The STNV leader and TED have two regions of complementarity. One of the complementary regions in TED resembles picornavirus box A, which is involved in cap-independent translation but which is located upstream of the coding region.


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