Noncatalytic domains in DNA glycosylases | Sciact - научная деятельность

Noncatalytic domains in DNA glycosylases Научная публикация

Журнал

International Journal of Molecular Sciences
, E-ISSN: 1422-0067

Вых. Данные

Год: 2022, Том: 23, Номер: 13, Номер статьи : 7286, Страниц : DOI: 10.3390/ijms23137286

Ключевые слова

base excision repair; DNA binding; DNA glycosylases; DNA repair; intrinsically disordered protein regions; lesion search in DNA; noncatalytic protein domains; post-translational modifications; protein–protein interactions

Авторы

Torgasheva Natalia A. ¹ , Diatlova Evgeniia A. ^1,2 , Grin Inga R. ¹ , Endutkin Anton V. ¹ , Mechetin Grigory V. ¹ , Vokhtantsev Ivan P. ^1,2 , Yudkina Anna V. ¹ , Zharkov Dmitry O. ^1,2

Организации

1	Институт химической биологии и фундаментальной медицины СО РАН
2	Новосибирский государственный университет

Histones play important roles in chromatin functioning and gene transcription, but in the intercellular space, they are harmful since they stimulate systemic inflammatory and toxic responses. Electrophoretically homogeneous IgGs against myelin basic protein (MBP), as well as H3 and H4 histones, were isolated from sera of HIV-infected patients. In contrast to known classical proteases, these IgGs split exclusively only histones and MBP but no other control proteins. Among 13 sites of hydrolysis of H3 by IgGs against H3 and 14 sites for anti-MBP IgGs, only two sites of the hydrolysis were the same. Between seven cleavage sites of H4 with IgGs against H4 and 9 sites of this histone hydrolysis by antibodies against MBP, only three sites were the same. The sites of hydrolysis of H3 (and H4) with abzymes against these histones and against MBP were different, but several expended protein clusters containing hydrolysis sites are partially overlapped. The existence of enzymatic cross-reactivity of abzymes against H3 and H4 and MBP represents a great menace to humans since due to cell apoptosis, histones constantly occur in human blood. They can hydrolyze MBP of the myelin sheath of axons and play a negative role in the pathogenesis of HIV-infected patients.

Torgasheva N.A. , Diatlova E.A. , Grin I.R. , Endutkin A.V. , Mechetin G.V. , Vokhtantsev I.P. , Yudkina A.V. , Zharkov D.O.
Noncatalytic domains in DNA glycosylases
International Journal of Molecular Sciences. 2022. Т.23. №13. 7286 . DOI: 10.3390/ijms23137286 WOS Scopus OpenAlex

Опубликована в печати:

30 июн. 2022 г.

Web of science:	WOS:000825697400001
Scopus:	2-s2.0-85133136227
OpenAlex:	W4283742826

БД	Цитирований
Scopus	1
OpenAlex	3
Web of science	3