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  • Title: cDNA cloning of rat liver 2,4-dienoyl-CoA reductase.
    Author: Hirose A, Kamijo K, Osumi T, Hashimoto T, Mizugaki M.
    Journal: Biochim Biophys Acta; 1990 Jul 30; 1049(3):346-9. PubMed ID: 2383590.
    Abstract:
    cDNA clones of 2,4-dienoyl-CoA reductase were isolated from rat liver cDNA libraries constructed in phages lambda gt11 and lambda gt10. Hybrid selected translation analysis revealed that 2,4-dienoyl-CoA reductase was translated as a polypeptide with a molecular weight of about 36,000, which was about 3,000 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 = 36,132), 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.
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