Primary structure of the two variants of Xenopus laevis mtSSB, a mitochondrial DNA binding protein

The primary structure of the single-stranded DNA binding protein from Xenopus laevis oocyte mitochondria (mtSSB) has been determined by Edman degradation of the intact molecule and peptides derived from partial α-chymotrypsin proteolysis and enzymatic cleavage with trypsin and endoproteinase Glu-C....

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Veröffentlicht in:Archives of biochemistry and biophysics 1991-12, Vol.291 (2), p.395-400
Hauptverfasser: Ghrir, Rachid, Lecaer, Jean-Pierre, Dufresne, Catherine, Gueride, Monique
Format: Artikel
Sprache:eng
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Zusammenfassung:The primary structure of the single-stranded DNA binding protein from Xenopus laevis oocyte mitochondria (mtSSB) has been determined by Edman degradation of the intact molecule and peptides derived from partial α-chymotrypsin proteolysis and enzymatic cleavage with trypsin and endoproteinase Glu-C. The native mtSSB is composed of two related polypeptide chains, mtSSBs and mtSSBr. The sequence of mtSSBs consists of 129 amino acids with a calculated molecular mass of 14,627 Da. Comparison of the first 80 residues of the two chains reveals 91% identity. A high degree of similarity is found between mtSSB and Escherichia coli SSB or F sex factor SSB.
ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(91)90152-9