Processing of the encephalomyocarditis virus capsid precursor protein studied in rabbit reticulocyte lysates incubated with N-formyl-[35S]methionine-tRNAfMet.
Translation of encephalomyocarditis virus RNA in rabbit reticulocyte lysates in the presence of N-formyl-[(35)S]methionine-tRNA(f) (Met) 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.
D000818:Animals; D002213:Capsid / Q000378:metabolism*; D004686:Encephalomyocarditis virus / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012346:RNA, Transfer, Amino Acyl; D012358:RNA, Transfer, Met; D011817:Rabbits; D012156:Reticulocytes; D013462:Sulfur Radioisotopes; D014764:Viral Proteins / Q000378:metabolism*
D011498:Protein Precursors; D012346:RNA, Transfer, Amino Acyl; D012358:RNA, Transfer, Met; D013462:Sulfur Radioisotopes; D014764:Viral Proteins; C024988:tRNA, formylmethionine-; D010447:Peptide Hydrolases