title: [Possibility of participation of proteins binding single-stranded DNA in eukaryotic DNA replication].
abstract: Main properties of the single-stranded DNA-binding proteins (SSB-proteins) (type of the protein UP 1 from the calf thymus) have been analyzed. The combination of some properties allows one to say about the strong specificity of the term "SSB-proteins type UP 1" and their differences from the HMG-proteins and other DNA-binding proteins and enzymes. Basing on the data from literature and the author's data the hypothesis was made that eukaryotic SSB-proteins may be involved in DNA replication, though they have tight relationship with the proteins of heterogeneous nuclear ribonucleoprotein particles. The following fact evidence for the involvement of SSB-proteins in DNA replication: 1) preferential affinity to the single-strand DNA in comparison with the single-strand RNA; 2) the contact between DNA SSB-proteins in chromatin; 3) strong proportional dependence between the content of SSB-proteins in chromatin and the intensity of DNA synthesis; 4) the dependence between the content of SSB-proteins in the cells and genomic size in different organisms; 5) the capacity of SSB-proteins to specific stimulation of DNA replicative synthesis. Apparently SSB-proteins in chromatin modulate the replication with the aid of the unwinding of DNA, stabilizing of the single-strand region in this molecule and the activation of the DNA synthesis carried out by DNA polymerase.
authors.forename: A N
authors.initials: AN
authors.lastname: Koterov
mesh_terms: D000818:Animals; D004261:DNA Replication; D004277:DNA, Single-Stranded / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000502:physiology*; D005057:Eukaryotic Cells / Q000378:metabolism*; D006801:Humans; D012261:Ribonucleoproteins / Q000378:metabolism
chemical_list: D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D012261:Ribonucleoproteins
vernacular_title: Vozmozhnost' uchastiia belkov, sviazyvaiushchikhsia s odnonitevoĭ DNK, v replikatsii DNK u éukariot.