Characterization of a mitochondrial protein binding to single-stranded DNA
- 1 January 1985
- journal article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 13 (5) , 1703-1716
- https://doi.org/10.1093/nar/13.5.1703
Abstract
A DNA-binding protein from Xenopus laevis oocyte mitochondria which has been found associated with the D-loop also shows a strong preference for single-stranded DNA. The binding to polynucleotides is dependent on the base composition, but no sequence specificity was found. This protein, called mtSSB, binds tightly and cooperatively to single-stranded DNA. By its amino-acid composition and its binding properties it appears to be similar to the single-stranded DNA-binding proteins found in prokaryotes.Keywords
This publication has 36 references indexed in Scilit:
- Co-linear organization of Xenopus laevis and mouse mitochondrial genomesBiochemical and Biophysical Research Communications, 1984
- Mitochondrial DNA-binding proteins that bind preferentially to supercoiled molecules containing the D-loop region of Xenopus laevis mtDNABiochemical and Biophysical Research Communications, 1983
- On the determination of deoxyribonucleic acid-protein interaction parameters using the nitrocellulose filter-binding assayBiochemistry, 1983
- Isolation of a yeast single-strand deoxyribonucleic acid binding protein that specifically stimulates yeast DNA polymerase IBiochemistry, 1983
- Nucleotide sequence of bacteriophage λ DNAJournal of Molecular Biology, 1982
- Primary structure of the histone H2A and H2B genes and their flanking sequences in a minor histone gene cluster of Xenopus laevisFEBS Letters, 1982
- Primary structure of the histone H3 and H4 genes and their flanking sequences in a minor histone gene cluster of Xenopus laevisFEBS Letters, 1981
- Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencingJournal of Molecular Biology, 1980
- A method for the fractionation of the high-mobility-group non-histone chromosomal proteinsBiochemical and Biophysical Research Communications, 1977
- The amino acid sequence of a DNA binding protein, the gene 5 product of fd filamentous bacteriophageFEBS Letters, 1974