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Интеллектуальная Система Тематического Исследования НАукометрических данных |
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Thymidine glycol: the effect on DNA structure and DNA binding by site-specific proteinsстатья
- Авторы: Kubareva E.A., Yang F., Ryazanova A.Yu, Dolinnaya N.G., Golovin A.V., Molochkov N.V., Romanova E.A., Karpova E.A., Zatsepin T.S., Oretskaya T.S.
- Журнал: Natural Science
- Том: 7
- Номер: 11
- Год издания: 2015
- Первая страница: 491
- Последняя страница: 509
- DOI: 10.4236/ns.2015.711051
- Аннотация: Thymidine glycol (5,6-dihydroxy-5,6-dihydrothymidine, Tg) is a major type of oxidative damage in DNA. Here we show that Tg residue in DNA duplex affects the local duplex structure depending on the sequence context around the Tg lesion. Circular dichroism spectra indicate that the local conformational change is transmitted to the neighboring base pairs. Molecular dynamics simulations demonstrate that Tg is partially out of the double helix. For the first time, Tg impact on several site-specific DNA-binding proteins is studied, namely p50 and p65 subunits of nuclear factor kappa-B (NF-κB) and DNA methyltransferase SsoII (M.SsoII). Our results show that p50/p50 and p65/p65 homodimers of NF-κB can tolerate a single Tg residue in the binding site quite well. Nevertheless the homodimers have different affinity to the oxidized variants of the κB site depending on the Tg position. M.SsoII can act as a transcription repressor when bound to the so-called regulatory site. M.SsoII demonstrates decreased affinity and lowered methylation efficiency when its methylation site contains Tg in the central position. Single Tg in one half of the regulatory site decreases M.SsoII affinity to the oxidized DNA whereas Tg presence in both half-sites prevents M.SsoII binding to such ligand.
- Добавил в систему: Романова Елена Александровна
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | Natural_Science.pdf | 1,5 МБ | 14 июня 2016 [KubarevaEA] |