Leucyl, phenylalanyl-tRNA-protein transferase also catalyzes transfer of methionyl residues as indicated by (i) copurification over a 1000-fold range of transfer activities for all three amino acids and (ii) loss of methionyl transfer activity in a mutant of E. coli lacking the transferase and reappearance of this activity in a transferase revertant. The purified enzyme was found to use Met-tRNAmMet in preference to Met-tRNAfMet as donor substrate. Peptides containing a basic amino acid at the NH2-terminus functioned as acceptors for the transfer of methionyl residues.
|Original language||English (US)|
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jul 26 1976|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology