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Amino-acid sequence of the signal peptide of mitochondrial nicotinamide nucleotide transhydrogenase as determined from the sequence of its messenger-rna

Academic Article
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Overview

authors

  • Yamaguchi, M.
  • Hatefi, Y.
  • Trach, K.
  • Hoch, James

publication date

  • November 1988

journal

  • Biochemical and Biophysical Research Communications  Journal

abstract

  • The amino acid sequence of the bovine mitochondrial nicotinamide nucleotide transhydrogenase was recently deduced from isolated cDNAs and reported [Yamaguchi, M., Hatefi, Y., Trach, K., and Hoch, J.A. (1988) J. Biol. Chem. 263, 2761-2767]. The cDNAs lacked the N-terminal coding region, however, and the 8 N-terminal residues were determined by protein sequencing. In the present study, the nucleotide sequence of the 5' upstream region was determined by dideoxynucleotide sequencing of the transhydrogenase messenger RNA, and amino acid sequences of the N-terminal region and the signal peptide of the enzyme were deduced from the nucleotide sequence. The N-terminal sequence of the enzyme as deduced from the mRNA sequence is the same as that determined by protein sequencing, with one difference. Protein sequencing showed Ser as the N-terminal residue. The mRNA sequence indicated that Ser is the second N-terminal residue, and the first is Cys. That preparations of the enzyme are mixtures of two polypeptides, one polypeptide being one residue shorter at the N terminus than the other, has been pointed out in the above reference. The signal peptide consists of 43 residues, is rich in basic (4 Lys, 2 Arg) and hydroxylated (4 Thr, 3 Ser) amino acids, and lacks acidic residues.

subject areas

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • Membrane Proteins
  • Mitochondria, Heart
  • Molecular Sequence Data
  • NADH, NADPH Oxidoreductases
  • NADP Transhydrogenases
  • Protein Sorting Signals
  • RNA, Messenger
  • Solubility
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Identity

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1016/s0006-291x(88)80005-6

PubMed ID

  • 3196335
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Additional Document Info

start page

  • 24

end page

  • 29

volume

  • 157

issue

  • 1

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