Proteolytic origin of the 150-kilodalton protein encoded by turnip yellow mosaic virus genomic RNA

Turnip yellow mosaic virus genomic RNA codes in vitro for two overlapping proteins, 150-kilodalton (150K protein) and 206-kilodalton (206K protein) proteins. The proteolytic maturation known to affect the 206K protein has been further characterized by in vitro translation assays in a reticulocyte ly...

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Bibliographic Details
Published inJournal of Virology Vol. 63; no. 12; pp. 5153 - 5158
Main Authors Morch, M.D. (Institut Jacques Monod, Paris, France), Drugeon, G, Szafranski, P, Haenni, A.L
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for Microbiology 01.12.1989
Subjects
ARN
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Gene Expression
Genes, Viral
GENOMAS
GENOME
INHIBIDORES DE ENZIMAS
INHIBITEUR D'ENZYME
Kinetics
Microbiology
Molecular Weight
Mosaic Viruses - genetics
Peptide Hydrolases - metabolism
PROTEASAS
PROTEASE
Protease Inhibitors - pharmacology
Protein Biosynthesis
PROTEINAS
PROTEINE
PROTEOLISIS
PROTEOLYSE
Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains
RNA, Viral - genetics
TEMPERATURA
TEMPERATURE
Thermodynamics
turnip yellow mosaic virus
Viral Proteins - genetics
Viral Structural Proteins - genetics
Virology
VIRUS DE LAS PLANTAS
VIRUS DES VEGETAUX
Temperature
Molecular processing
In vitro translation
RNA
Gel electrophoresis
Enzyme
Turnip yellow mosaic virus
Proteinase
Enzyme inhibitor
Phytopathogen
Virus
Proteins
Tymovirus
Proteolysis
Cleavage
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Summary:Turnip yellow mosaic virus genomic RNA codes in vitro for two overlapping proteins, 150-kilodalton (150K protein) and 206-kilodalton (206K protein) proteins. The proteolytic maturation known to affect the 206K protein has been further characterized by in vitro translation assays in a reticulocyte lysate or wheat germ extract. Cleavage is inhibited at 37 degrees C and restored when the temperature is shifted to 30 or 25 degrees C. Temperature shift experiments are used here to demonstrate that the 150K protein and the previously characterized 78K protein are the two fragments resulting from a primary cleavage phenomenon that affects the 206K protein in a cotranslational manner under usual translation conditions. This processing isprevented by several cysteine and serine proteinase inhibitors
Bibliography:H20
9021262
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ISSN:0022-538X
1098-5514
DOI:10.1128/jvi.63.12.5153-5158.1989