Efficient Ribosome Binding of Brome Mosaic Virus (BMV) RNA4 Contributes to Its Ability to Outcompete the Other BMV RNAs for Translation

Autor:	John W. Pyne, Timothy C. Hall
Rok vydání:	1979
Předmět:	Peptide Biosynthesis Cell-Free System biology viruses food and beverages Hordeum Translation (biology) Coat protein biology.organism_classification Virology Ribosome Molecular Weight Viral Proteins Infectious Diseases Brome mosaic virus Mosaic Viruses Protein Biosynthesis RNA Viral Ribosomes
Zdroj:	Intervirology. 11:23-29
ISSN:	1423-0100 0300-5526
DOI:	10.1159/000149008
Popis:	Analysis of translation products synthesized in vitro in the presence of a mixture of brome mosaic virus (BMV) RNAs 1, 2, 3, and 4 usually shows a predominance of coat protein, coded by RNA4. The proportion of products directed by RNAs 1 and 2 decreased at saturating concentrations of BMV RNA and in the presence of 7-methylguanosine 5'-phosphate (m7G5'p) at nonsaturating concentrations of RNA. No differences in the relative proportions of the various proteins produced were detected in the presence of T-2 toxin, which interferes with the formation of the first peptidyl bond rather than competing for initiation factor, as has been suggested for m7G5'p. These data show that the ability of BMV RNA4 to outcompete BMV RNAs 1, 2, and 3 results, at least in part, from its ability to bind more efficiently to ribosomes.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::391a34ed4f33e966c88c0a180a2b01c8 https://doi.org/10.1159/000149008 Zobrazit plný text záznamu