Literature DB >> 3038094

Molecular cloning and sequence analysis of full-length cDNA for mRNA of adrenodoxin oxidoreductase from bovine adrenal cortex.

Y Nonaka, H Murakami, Y Yabusaki, S Kuramitsu, H Kagamiyama, T Yamano, M Okamoto.   

Abstract

A full-length cDNA clone (pADR) for adrenodoxin reductase was isolated by means of immunological screening from a bovine adrenal poly(A)+ mRNA library. A cDNA insert of 1,973 base pairs in length encoded the entire amino acid sequence of the adrenodoxin reductase precursor protein, which consists of 492 amino acids including an extrapeptide of 32 amino acids at the NH2-terminus. The cloned cDNA contained the complete 3'-noncoding region of 443 nucleotides including 59 nucleotides of poly(A) and 51 nucleotides in the 5'-noncoding region. The amino acid sequences from the 33rd to 70th, the 117th to 123rd, the 207th to 225th, the 247th to 323rd, the 385th to 426th, the 444th to 461st, and the 487th to 492nd in the predicted structure were identical with those of the purified adrenodoxin reductase and its digested peptides, with only four exceptions.

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Year:  1987        PMID: 3038094     DOI: 10.1016/0006-291x(87)91570-1

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Identification and molecular characterization of mitochondrial ferredoxins and ferredoxin reductase from Arabidopsis.

Authors:  Keiko Takubo; Tomomi Morikawa; Yasuki Nonaka; Masaharu Mizutani; Shigeo Takenaka; Keiji Takabe; Masa-aki Takahashi; Daisaku Ohta
Journal:  Plant Mol Biol       Date:  2003-07       Impact factor: 4.076

2.  Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif.

Authors:  J P Hendrick; P E Hodges; L E Rosenberg
Journal:  Proc Natl Acad Sci U S A       Date:  1989-06       Impact factor: 11.205

  2 in total

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