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PMID: 8139566 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

His-154 is involved in the linkage of the Saccharomyces cerevisiae L-A double-stranded RNA virus Gag protein to the cap structure of mRNAs and is essential for M1 satellite virus expression.

Molecular and cellular biology ·Vol. 14 ·No. 4 ·1994-04-00 ·Pages 2664-74

Blanc A, Ribas JC, Wickner RB, Sonenberg N

Abstract

The coat protein (Gag) of the double-stranded RNA virus L-A was previously shown to form a covalent bond with the cap structure of eukaryotic mRNAs. Here, we identify the linkage as a phosphoroimidazole bond between the alpha phosphate of the cap structure and a nitrogen in the Gag protein His-154 imidazole side chain. Mutations of His-154 abrogate the ability of Gag to bind to the cap structure, without affecting cap recognition, in vivo virus particle formation from an L-A cDNA clone, or in vitro specific binding and replication of plus-stranded single-stranded RNA. However, genetic analyses demonstrate that His-154 is essential for M1 satellite virus expression.

MeSH Terms
Amino Acid Sequence Base Sequence Gene Products, gag/biosynthesis,isolation & purification,metabolism Histidine Molecular Sequence Data Mutagenesis, Site-Directed Oligodeoxyribonucleotides Plasmids RNA Caps/isolation & purification,metabolism RNA, Double-Stranded/isolation & purification,metabolism RNA, Messenger/isolation & purification,metabolism Saccharomyces cerevisiae/genetics,metabolism Suppression, Genetic Virus Replication
Chemicals
Gene Products, gag Oligodeoxyribonucleotides RNA Caps RNA, Double-Stranded RNA, Messenger Histidine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Blanc A
Department of Biochemistry, McGill University, Montréal, Québec, Canada.
Ribas J C
Wickner R B
Sonenberg N
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.14.4.2664-2674.1994
Published
1994-04-00
Pages
2664-74
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC358633
Subset
IM
External Links
PubMed source DOI: 10.1128/mcb.14.4.2664-2674.1994 PMC Full Text View journal details
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