Nucleoside triphosphate dependent peptide activation by a crude soluble protein fraction of baker's yeast: A new type of activating mechanism

Abstract

The occurrence of carboxyl activated peptides in extracts of baker's yeast was reported by a group of workers from this laboratory about three years ago (Koningsberger et al., 1957 a, b). Adenosine-5'-monophosphate (v.d.Grinten, 1959; Koningsberger, 1959) and cytidine-5' -monophosphate (Schuurs et al., 1960) bound carboxyl activated peptides have been isolated and identified, as well as phosphate bound peptides without nucleotide material (de Kloet et al., 1960 b). Furthermore, it was shown that ribonucleic acid preparations from both soluble (s-RNA) and particulate ribonucleoprotein (m-RNA) fractions of yeast contain carboxyl activated peptides (de Kloet et al., 1960 a). Moreover, a number of similar nucleotide bound peptides has been isolated from various tissues and microorganisms synthesizing protein (e.g. Dirheimer et al., 1958; Harris et al., 1959; Hase et al., 1959). During a trial to study peptide activation (Tuboi et al., 1960) by a crude fraction of yeast soluble (100.000 g supernatant) protein a new type of energy-dependent hydroxamate formation was found to occur. In this paper, preliminary data