N. V. Belyakova

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Mammalian nuclear DNA polymerases alpha and beta are known to be devoid of the editing 3'-->5' exonucleolytic activity. Presumably this activity could be effected by the exonucleases non-associated covalently with DNA polymerases. Two 3'-->5' exonucleases of 40 kDa and 50 kDa (exo-40 and exo-5) have been isolated from rat liver nuclei and purified to near(More)
Autonomous 3'-->5'exonucleases are not bound covalently to DNA polymerases but are often involved in replicative complexes. Such exonucleases from rat liver, calf thymus and Escherichia coli (molecular masses of 28+/-2 kDa) are shown to increase more than 10-fold the accuracy of DNA polymerase beta (the most inaccurate mammalian polymerase) from rat liver(More)
Recently we have revealed a high content of autonomous 3"→5" exonucleases (AE), i.e., those not bound covalently with DNA polymerases, in cells of vertebrates, from fish to human [1]. In the present work, using gel filtration method, cell-free extracts were studied from 15 objects located at different positions on the phylogenetic tree, such as(More)
Huge range of concentrations of different protein and insufficient sensitivity of methods for detection of proteins at a single molecule level does not yet allow obtaining the whole image of human proteome. In our investigations, we tried to evaluate the size of different proteomes (cells and plasma). The approach used is based on detection of protein spots(More)
The complexes of repair DNA polymerase β with 3′-exonuclease and some other proteins were isolated from the chromatin of hepatocytes of normal rats for the first time. Biopolymers were extracted from the chromatin by the solution of NaCl and Triton X-100. The extract was fractionated by gel-filtration on Sephacryl S-300 columns successively in low and high(More)
The possibility of interaction of recombinant proteins of human repair DNA polymerase β with proofreading 3′ → 5′-exonucleases TREX1 and TREX2 was investigated in vitro for the first time. The results of gel filtration analysis show the formation of a complex between 3′ → 5′-exonucleases mTREX1 and hTREX2 and DNA polymerase β. DNA polymerase activity is(More)
The accuracy of DNA synthesis catalyzed by purified nuclear DNA polymerases is by five to seven orders of magnitude lower than the probability of spontaneous mutations [1]. Therefore, the vast majority of errors are corrected in vivo. Postreplicative repair of the errors of replication enhance the accuracy of the DNA synthesis only by one to three orders of(More)
A study was made of the correcting role of autonomous 3" → 5" exonucleases (AE) contained in multienzyme DNA polymerase complexes of rat hepatocytes or calf thymocytes. DNA was synthesized on phage φX174 amber3 or M13mp2 primer–templates, and used to transfect Escherichia coli spheroplasts. Frequencies were estimated for direct and reverse mutations(More)
Properties and mechanisms of PCNA (proliferating cell nuclear antigen) functions have been investigated for a long time and are studied in great detail. As follows from its name, most known PCNA functions (DNA replication, DNA repair, DNA recombination and others) are connected with cell proliferation and localization of this protein in nuclei. In addition,(More)
2',3'-Dideoxy-3'-aminonucleoside 5'-triphosphates are shown to be strong inhibitors of repair DNA synthesis in gamma-irradiated rat liver chromatin. The activity of these compounds is comparable with that of the most effective inhibitor of the DNA polymerase beta-catalyzed repair DNA synthesis.
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