Search

Your search keyword '"Oretskaya, Tatiana S."' showing total 18 results
Start Over Author "Oretskaya, Tatiana S." Search Limiters Available in Library Collection
18 results on '"Oretskaya, Tatiana S."'

1. 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
Full Text
View/download PDF

4. 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
Full Text
View/download PDF

14. Is Thymidine Glycol Containing DNA a Substrate of E. coli DNA Mismatch Repair System?

Author

Perevozchikova, Svetlana A., Trikin, Roman M., Heinze, Roger J., Romanova, Elena A., Oretskaya, Tatiana S., Friedhoff, Peter, and Kubareva, Elena A.

Subjects
ESCHERICHIA coli, THYMIDINE, DNA repair, DNA replication, FLUORESCENCE anisotropy, PLASMIDS
Abstract

The DNA mismatch repair (MMR) system plays a crucial role in the prevention of replication errors and in the correction of some oxidative damages of DNA bases. In the present work the most abundant oxidized pyrimidine lesion, 5,6-dihydro-5,6-dihydroxythymidine (thymidine glycol, Tg) was tested for being recognized and processed by the E. coli MMR system, namely complex of MutS, MutL and MutH proteins. In a partially reconstituted MMR system with MutS-MutL-MutH proteins, G/Tg and A/Tg containing plasmids failed to provoke the incision of DNA. Tg residue in the 30-mer DNA duplex destabilized double helix due to stacking disruption with neighboring bases. However, such local structural changes are not important for E. coli MMR system to recognize this lesion. A lack of repair of Tg containing DNA could be due to a failure of MutS (a first acting protein of MMR system) to interact with modified DNA in a proper way. It was shown that Tg in DNA does not affect on ATPase activity of MutS. On the other hand, MutS binding affinities to DNA containing Tg in G/Tg and A/Tg pairs are lower than to DNA with a G/T mismatch and similar to canonical DNA. Peculiarities of MutS interaction with DNA was monitored by Förster resonance energy transfer (FRET) and fluorescence anisotropy. Binding of MutS to Tg containing DNAs did not result in the formation of characteristic DNA kink. Nevertheless, MutS homodimer orientation on Tg-DNA is similar to that in the case of G/T-DNA. In contrast to G/T-DNA, neither G/Tg- nor A/Tg-DNA was able to stimulate ADP release from MutS better than canonical DNA. Thus, Tg residue in DNA is unlikely to be recognized or processed by the E. coli MMR system. Probably, the MutS transformation to active “sliding clamp” conformation on Tg-DNA is problematic. [ABSTRACT FROM AUTHOR]

Published
2014
Full Text
View/download PDF

17. Mechanistic comparison of Bacillus subtilis6S-1 and 6S-2 RNAs—commonalities and differences

Author

Burenina, Olga Y., Hoch, Philipp G., Damm, Katrin, Salas, Margarita, Zatsepin, Timofei S., Lechner, Marcus, Oretskaya, Tatiana S., Kubareva, Elena A., and Hartmann, Roland K.

Abstract

Bacteria synthesize small regulatory RNAs known as 6S RNAs which bind to RNA polymerase and regulate transcription. This paper describes an analysis of two 6S RNAs produced in Bacillus subtilis. Although these two RNAs share many features, there are also distinct differences, the mechanistic implications of which are discussed.

Published
2014
Full Text
View/download PDF

18. 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
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results