Primary structure of the two variants of Xenopus laevis mtSSB, a mitochondrial DNA binding protein |
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| Authors: | R Ghrir J P Lecaer C Dufresne M Gueride |
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| Institution: | Institut de Génétique et Microbiologie, Université Paris-Sud, Orsay, France. |
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| Abstract: | 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 alpha-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. |
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