Site-directed mutagenesis of basic amino acid residues in the extension peptide of P-450(SCC) precursor: Effects on the import of the precursor into mitochondria

Takeo Kumamoto, Ken-Ichirou Morohashi, Akio Ito, Tsuneo Omura

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

The precursor of cytochrome P-450(SCC) (preP-450(SCC)), an inner membrane protein of adrenal cortex mitochondria, has an extension peptide consisting of 39 amino acids which is thought to play an essential role in the import of the precursor into mitochondria. The amino terminal portion of the extension peptide contains three positively charged amino acid residues, Arg(4), Arg(9), and Lys(14). To investigate their role in the import of preP-450(SCC) into mitochondria, they were replaced by other amino acids, Ser or Thr, by site-directed mutagenesis. The import of mutated preP-450(SCC)s with single amino acid substitution was much less efficient than with the original precursor. The mutated preP-450(SCC)s with two or three substitutions were not imported. These results suggest that the positively charged amino acid residues in the amino terminal portion of the extension peptide are essential for the import of preP-450(SCC) into mitochondria.

Original languageEnglish
Pages (from-to)833-838
Number of pages6
JournalJournal of Biochemistry
Volume102
Issue number4
Publication statusPublished - Oct 1987

All Science Journal Classification (ASJC) codes

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Physiology (medical)
  • Radiology Nuclear Medicine and imaging
  • Molecular Biology
  • Biochemistry

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