Translational Readthrough of an Amber Termination Codon During Synthesis of Feline Leukemia Virus Protease

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 1985 Sep 1

PMID 2991607

Citations 44

Authors

Y Yoshinaka

I Katoh

T D Copeland

S Oroszlan

Affiliations

Soon will be listed here.

Abstract

Feline leukemia virus contains a protease which apparently has the same specificity as murine leukemia virus protease. It cleaves in vitro the Pr65gag of Gazdar-mouse sarcoma virus into the constituent p15, p12, p30, and p10 proteins. We purified the protease and determined its NH2-terminal amino acid sequence (the first 15 residues). Alignment of this amino acid sequence with the nucleotide sequence (I. Laprevotte, A. Hampe, C. H. Sherr, and F. Galibert, J. Virol. 50:884-894, 1984) reveals that the protease is a viral-coded enzyme and is located at the 5' end of the pol gene. As previously found for murine leukemia virus (Y. Yoshinaka, I. Katoh, T. D. Copeland, and S. Oroszlan, Proc. Natl. Acad. Sci. U.S.A. 82:1618-1622, 1985), feline leukemia virus protease is synthesized through in-frame suppression of the gag amber termination codon by insertion of a glutamine in the fifth position, and the first four amino acids are derived from the gag gene.

Citing Articles

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The functional readthrough extension of malate dehydrogenase reveals a modification of the genetic code.

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Translational readthrough-promoting drugs enhance pseudoknot-mediated suppression of the stop codon at the Moloney murine leukemia virus gag–pol junction.

Green L, Goff S J Gen Virol. 2015; 96(11):3411-3421.

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Nonsense suppression by near-cognate tRNAs employs alternative base pairing at codon positions 1 and 3.

Roy B, Leszyk J, Mangus D, Jacobson A Proc Natl Acad Sci U S A. 2015; 112(10):3038-43.

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Ribosome profiling reveals pervasive and regulated stop codon readthrough in Drosophila melanogaster.

Dunn J, Foo C, Belletier N, Gavis E, Weissman J Elife. 2013; 2:e01179.

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