Template-dependent polypeptide synthesis in a factor- and energy-free translation system promoted by pyridine

Itaru Nitta, Takuya Ueda, Takahiko Nojima, Kimitsuna Watanabe*

*この研究の対応する著者

研究成果: Article査読

3 被引用数 (Scopus)

抄録

We demonstrate here that a high concentration (40-70%) of pyridine, an aromatic tertiary amine catalyst, is able to promote translation on ribosomes without the presence of soluble protein factors or chemical energy sources. Compared with Monro's fragment reaction [Methods Enzymol. 20, 472-481 (1971)], which reflects only the peptidyltransferase step, this novel translation system can produce polypeptides with chain lengths of at least several tens of residues depending on the template RNA. In the presence of 60% pyridine, poly(U) and poly(UC) promoted incorporation of the respective amino acids, phenylalanine and serine-leucine, twofold, whereas poly(A) promoted the incorporation of lysine by only 25%. The degrees of polymerization of phenylalanine and lysine were up to the decamer and around 40mer, respectively. In poly(UC)-dependent oligo(serine-leucine) synthesis, oligo-peptides with a serine and leucine alternate sequence were the main products. This novel pyridine system evidently differs from the non-enzymatic translation system reported by Gavrilova and Spirin [FEBS Lett. 17, 324-326 (1971)]; the former system displays partial resistance toward deproteinization reagents such as SDS and proteinase K, whereas the latter system is completely sensitive.

本文言語English
ページ(範囲)841-849
ページ数9
ジャーナルJournal of biochemistry
118
4
DOI
出版ステータスPublished - 1995 10
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 分子生物学

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