Abstract
This paper presents a thorough analysis of the N-terminal amino acid sequence of the satellite tobacco necrosis virus (STNV) coat protein produced by translation of STNV ribonucleic acid in an in vitro wheat embryo system. Short term incubations detect a limited incorporation of [35S]methionine from [35S]Met-tRNAMiMet. This incorporated [35S]Met is largely lost on prolonged incorporation. Sucrose gradient analysis of protein synthesis initiation complexes of [3H]Met-tRNAiMet, STNV-RNA, and wheat embryo ribosomes demonstrate that formation of the complexes requires the methionine-specific initiator tRNA. Electrophoretic resolution of labeled products found in these complexes detects the STNV-RNA dependent production of the peptide Met-Ala-Lys and its precursors. Comparison of this apparent N-terminal sequence with the Ala-Lys t N-terminal sequence of in vivo STNV coat protein dictates that STNV-RNA translation by an in vitro procaryotic system in that correct translation begins on a Met codon immediately prior to the codons governing the final in vivo sequence.
Original language | English (US) |
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Pages (from-to) | 1528-1531 |
Number of pages | 4 |
Journal | Biochemistry |
Volume | 12 |
Issue number | 8 |
DOIs | |
State | Published - Apr 1 1973 |
ASJC Scopus subject areas
- Biochemistry