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- W2083127734 abstract "The studies presented were undertaken to clarify the unsettled question whether the synthesis of histones with a N-acetylserine residue at the amino terminal end is initiated with methionine. Histones were synthesized in vitro in a rabbit reticulocyte lysate, primed with a mRNA preparation from ascites cells. Initiation of polypeptide synthesis was investigated by using N-formyl[35S]met-tRNAfMet from yeast to label the N-termini. N-Formylmethionine was incorporated into histones H1 and H4 whose N-terminal amino acid is alpha-N-acetylserine. By comparison of tryptic peptides derived from these two histones labeled either with methionine or formylmethionine and from Edman degradation it is shown that N-terminal acetylated histones are initiated with methionine, as is the case for other eukaryotic and bacterial proteins." @default.
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- W2083127734 date "1976-06-15" @default.
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- W2083127734 title "Initiation of synthesis of N-terminal acetylated histones with methionine" @default.
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- W2083127734 doi "https://doi.org/10.1021/bi00657a008" @default.
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