cDNA cloning of rat liver 2,4-dienoyl-CoA reductase

Akihiko Hirose, Keiju Kamijo, Takashi Osumi, Takashi Hashimoto, Michinao Mizugaki

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)

Abstract

cDNA clones of 2,4-dienoyl-CoA reductase were isolated from rat liver cDNA libraries constructed in phages λgt11 and λgt10. Hybrid selected translation analysis revealed that 2,4-dienoyl-CoA reductase was translated as a polypeptide with a molecular weight of about 36000, which was about 3000 molecular weight units larger than mature reductase. Sequencing analysis revealed that the open reading frame encoded a polypeptide consisting of 335 amino acid residues (predicted molecular weight = 36132), which contained an N-terminal extension peptide of 34 amino acid residues (presequence) in addition to the mature enzyme. Thus, 2,4-dienoyl-CoA reductase is synthesized as a larger precursor polypeptide, and the N-terminal extension peptide may be acting as the mitochondrial import signal.

Original languageEnglish
Pages (from-to)346-349
Number of pages4
JournalBBA - Gene Structure and Expression
Volume1049
Issue number3
DOIs
Publication statusPublished - 1990 Jul 30

Keywords

  • (Peroxisomal mitochondria)
  • 2,4-Dienoyl-CoA reductase
  • Phage λgt10
  • Phage λgt11
  • cDNA

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

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