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Your search keyword '"Oretskaya, Tatiana S."' showing total 12 results
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12 results on '"Oretskaya, Tatiana S."'

3. Reactive Acrylamide-Modified DNA Traps for Accurate Cross-Linking with Cysteine Residues in DNA–Protein Complexes Using Mismatch Repair Protein MutS as a Model

Author

Monakhova, Mayya V., primary, Kubareva, Elena A., additional, Kolesnikov, Kirill K., additional, Anashkin, Viktor A., additional, Kosaretskiy, Egor M., additional, Zvereva, Maria I., additional, Romanova, Elena A., additional, Friedhoff, Peter, additional, Oretskaya, Tatiana S., additional, and Zatsepin, Timofei S., additional

Published
2022
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6. Responses of DNA Mismatch Repair Proteins to a Stable G-Quadruplex Embedded into a DNA Duplex Structure

Author

Pavlova, Anzhela V., primary, Monakhova, Mayya V., additional, Ogloblina, Anna M., additional, Andreeva, Natalia A., additional, Laptev, Gennady Yu., additional, Polshakov, Vladimir I., additional, Gromova, Elizaveta S., additional, Zvereva, Maria I., additional, Yakubovskaya, Marianna G., additional, Oretskaya, Tatiana S., additional, Kubareva, Elena A., additional, and Dolinnaya, Nina G., additional

Published
2020
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8. DNA Polymerases β and λ Bypass Thymine Glycol in Gapped DNA Structures

Author

Belousova, Ekaterina A., Maga, Giovanni, Fan, Yang, Kubareva, Elena A., Romanova, Elena A., Lebedeva, Natalia A., Oretskaya, Tatiana S., and Lavrik, Olga I.

Abstract

Here we investigated the ability of the human X-family DNA polymerases β and λ to bypass thymine glycol (Tg) in gapped DNA substrates with the damage located in a defined position of the template strand. Maximum velocities and the Michaelis constant values were determined to study DNA synthesis in the presence of either Mg2+or Mn2+. Additionally, the influence of hRPA (human replication protein A) and hPCNA (human proliferating cell nuclear antigen) on TLS (translesion synthesis) activity of DNA polymerases β and λ was examined. The results show that (i) DNA polymerase λ is able to catalyze DNA synthesis across Tg, (ii) the ability of DNA polymerase λ to elongate from a base paired to a Tg lesion is influenced by the size of the DNA gap, (iii) hPCNA increases the fidelity of Tg bypass and does not influence normal DNA synthesis catalyzed by DNA polymerase λ, (iv) DNA polymerase β catalyzes the incorporation of all four dNTPs opposite Tg, and (v) hPCNA as well as hRPA has no specific effect on TLS in comparison with the normal DNA synthesis catalyzed by DNA polymerase β. These results considerably extend our knowledge concerning the ability of specialized DNA polymerases to cope with a very common DNA lesion such as Tg.

Published
2024
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11. Kinetic Basis of the Bifunctionality of SsoII DNA Methyltransferase.

Author

Timofeyeva, Nadezhda A., Ryazanova, Alexandra Yu., Norkin, Maxim V., Oretskaya, Tatiana S., Fedorova, Olga S., Kubareva, Elena A., and Iwahara, Junji

Subjects
METHYLTRANSFERASES, TRANSMETHYLATION, DNA, METHYLATION, ANTIVIRAL agents
Abstract

Type II restriction–modification (RM) systems are the most widespread bacterial antiviral defence mechanisms. DNA methyltransferase SsoII (M.SsoII) from a Type II RM system SsoII regulates transcription in its own RM system in addition to the methylation function. DNA with a so-called regulatory site inhibits the M.SsoII methylation activity. Using circular permutation assay, we show that M.SsoII monomer induces DNA bending of 31° at the methylation site and 46° at the regulatory site. In the M.SsoII dimer bound to the regulatory site, both protein subunits make equal contributions to the DNA bending, and both angles are in the same plane. Fluorescence of TAMRA, 2-aminopurine, and Trp was used to monitor conformational dynamics of DNA and M.SsoII under pre-steady-state conditions by stopped-flow technique. Kinetic data indicate that M.SsoII prefers the regulatory site to the methylation site at the step of initial protein–DNA complex formation. Nevertheless, in the presence of S-adenosyl-l-methionine, the induced fit is accelerated in the M.SsoII complex with the methylation site, ensuring efficient formation of the catalytically competent complex. The presence of S-adenosyl-l-methionine and large amount of the methylation sites promote efficient DNA methylation by M.SsoII despite the inhibitory effect of the regulatory site. [ABSTRACT FROM AUTHOR]

Published
2018
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12. Structure and function analysis of protein – nucleic acid complexes

Author

Kuznetsova, Svetlana A. and Oretskaya, Tatiana S.

Abstract

The review summarizes published data on the results and achievements in the field of structure and function analysis of protein – nucleic acid complexes by means of main physical and biochemical methods, including X-ray diffraction, nuclear magnetic resonance spectroscopy, electron and atomic force microscopy, small-angle X-ray and neutron scattering, footprinting and cross-linking. Special attention is given to combined approaches. The advantages and limitations of each method are considered, and the prospects of their application for wide-scale structural studies in vivoare discussed.

Published
2016
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