Role of basic amino acids in the cleavage of synthetic peptide substrates by mitochondrial processing peptidase

Myeong Cheol Song, Kunitoshi Shimokata, Sakae Kitada, Tadashi Ogishima, Akio Ito

研究成果: ジャーナルへの寄稿学術誌査読

31 被引用数 (Scopus)

抄録

Our recent experiments using model peptides of rat malate dehydrogenase (MDH) indicated that a proximal arginine and a distal basic amino acid are important for processing by mitochondrial processing peptidase (MPP). To elucidate if the recognition elements apply to other precursor proteins, we analyzed cleavage of model peptides of human ornithine aminotransferase (OAT). Purified peptidase cleaved peptides that corresponded to N-terminal 1-25 and 3-25 at the correct site (Gly17-Val18) at nearly equal rates. Replacement of Arg15 (-2 position) with lysine or alanine reduced the processing efficiency by 95- and 380-fold, respectively. Either deletion from Met1 to Arg10 or replacement of the basic amino acids between them decreased the processing efficiency considerably. A peptide containing Arg7 in addition to Lys4 and Arg10 was more effective than the control peptide. However, a peptide with one and two consecutive basic amino acids in the distal region had a processing efficiency close to the control peptide. These results indicated that processing of OAT was enhanced by an increase in the number of basic amino acids with a suitable distance between them. In other respects, the processing signal of OAT was essentially the same as that of MDH.

本文言語英語
ページ(範囲)1163-1166
ページ数4
ジャーナルJournal of biochemistry
120
6
DOI
出版ステータス出版済み - 1月 1 1996

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学

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