title: Amino terminal sequence of the mitochondrial protein mtDBP-C: similarity with nonhistone chromosomal proteins HMG 1 and 2.
abstract: We have previously reported the characterization of a DNA-binding protein isolated from Xenopus laevis mitochondria (mtDBP-C). The amino terminal sequence of this protein (26 residues) has been determined by automated Edman degradation and used to search for sequence similarity with the NBRF library. A segment of 17 amino acids displays 47.1% of identity with proteins HMG-1 and 2 of various vertebrate species.
authors.affiliation: Laboratoire de Biologie, INRST, Hammam-Lif, Tunisia.
authors.forename: R
authors.initials: R
authors.lastname: Ghrir
authors.forename: B
authors.initials: B
authors.lastname: Mignotte
authors.forename: M
authors.initials: M
authors.lastname: Guéride
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004268:DNA-Binding Proteins / Q000737:chemistry*; D005260:Female; D006609:High Mobility Group Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D012689:Sequence Homology, Nucleic Acid; D029867:Xenopus Proteins; D014982:Xenopus laevis
chemical_list: D004268:DNA-Binding Proteins; D006609:High Mobility Group Proteins; D029867:Xenopus Proteins; C072221:mitochondrial protein mtDBP-C, Xenopus