Processing of the Encephalomyocarditis Virus Capsid Precursor Protein Studies in Rabbit Reticulocyte Lysates Incubated with N-Formyl-[35S]Methionine-tRNAfMet
AUTOR(ES)
Campbell, Elizabeth A.
RESUMO
Translation of encephalomyocarditis virus RNA in rabbit reticulocyte lysates in the presence of N-formyl-[35S]methionine-tRNAfMet revealed that a small polypeptide is cleaved from the N-terminus of the capsid protein precursor, preA, by virus-coded protease activity. Therefore, this N-terminal segment comprising the translation initiation site is not conserved in any of the mature capsid proteins.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=256426Documentos Relacionados
- Cleavage of the Capsid Protein Precursors of Encephalomyocarditis Virus in Rabbit Reticulocyte Lysates
- Regulation of protein synthesis in rabbit reticulocyte lysates by the heme-regulated protein kinase: Inhibition of interaction of Met-tRNAfMet binding factor with another initiation factor in formation of Met-tRNAfMet·40S ribosomal subunit complexes
- Studies with [35S]methionine indicate that the 22,000-dalton [Met]enkephalin-containing protein in chromaffin cells is a precursor of [Met]enkephalin.
- Rapid method for the preparation of encephalomyocarditis virus protease from rabbit reticulocyte lysates.
- Regulation of protein synthesis in rabbit reticulocyte lysates: characteristics of inhibition of protein synthesis by a translational inhibitor from heme-deficient lysates and its relationship to the initiation factor which binds Met-tRNAf.
