Translation of satellite tobacco necrosis virus ribonucleic acid. I. Characterization of in vitro procaryotic and eucaryotic translation products

Biochemistry ◽  
1972 ◽  
Vol 11 (11) ◽  
pp. 2009-2014 ◽  
Author(s):  
William H. Klein ◽  
Chris Nolan ◽  
Jerome M. Lazar ◽  
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 ◽  
1976 ◽  
Vol 15 (22) ◽  
pp. 4943-4950 ◽  
Author(s):  
David W. Leung ◽  
Carl W. Gilbert ◽  
Robert E. Smith ◽  
Nancy L. Sasavage ◽  
John M. Clark

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.


2010 ◽  
Vol 155 (6) ◽  
pp. 999-1001
Author(s):  
Laszlo Krizbai ◽  
Maria Nemeth ◽  
Vivian Law ◽  
Christopher Reed ◽  
Aniko Varga ◽  
...  

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