Small-Angle X-Ray Characterization of the Nucleoprotein Complexes Resulting from DNA-Induced Oligomerization of HIV-1 Integrase Научная публикация
Журнал |
Nucleic Acids Research
ISSN: 0305-1048 , E-ISSN: 1362-4962 |
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Вых. Данные | Год: 2007, Том: 35, Номер: 3, Страницы: 975-987 Страниц : 13 DOI: 10.1093/nar/gkl1111 | ||||||
Ключевые слова | IMMUNODEFICIENCY-VIRUS TYPE-1; RESOLVED FLUORESCENCE ANISOTROPY; CARBOXYL-TERMINAL DOMAINS; VIRAL-DNA; CRYSTAL-STRUCTURE; RETROVIRAL DNA; BINDING; PROTEIN; CORE; MULTIMERIZATION | ||||||
Авторы |
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Организации |
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Информация о финансировании (6)
1 | Российский фонд фундаментальных исследований | 03-04-49781 |
2 | Сибирское отделение Российской академии наук | |
3 | University of Bordeaux | |
4 | Президиум РАН | 10.5 |
5 | French National Centre for Scientific Research | |
6 | Agence Nationale de Recherches sur le Sida et les Hépatites Virales |
Реферат:
HIV-1 integrase (IN) catalyses integration of a DNA copy of the viral genome into the host genome. Specific interactions between retroviral IN and long terminal repeats (LTR) are required for this insertion. To characterize quantitatively the influence of the determinants of DNA substrate specificity on the oligomerization status of IN, we used the small-angle X-ray scattering (SAXS) technique. Under certain conditions in the absence of ODNs IN existed only as monomers. IN preincubation with specific ODNs led mainly to formation of dimers, the relative amount of which correlated well with the increase in the enzyme activity in the 3'-processing reaction. Under these conditions, tetramers were scarce. Non-specific ODNs stimulated formation of catalytically inactive dimers and tetramers. Complexes of monomeric, dimeric and tetrameric forms of IN with specific and non-specific ODNs had varying radii of gyration (R-g), suggesting that the specific sequence-dependent formation of IN tetramers can probably occur by dimerization of two dimers of different structure. From our data we can conclude that the DNA-induced oligomerization of HIV-1 IN is probably of importance to provide substrate specificity and to increase the enzyme activity.
Библиографическая ссылка:
Baranova S.
, Tuzikov F.V.
, Zakharova O.D.
, Tuzikova N.A.
, Calmels C.
, Litvak S.
, Tarrago-Litvak L.
, Parissi V.
, Nevinsky G.A.
Small-Angle X-Ray Characterization of the Nucleoprotein Complexes Resulting from DNA-Induced Oligomerization of HIV-1 Integrase
Nucleic Acids Research. 2007. V.35. N3. P.975-987. DOI: 10.1093/nar/gkl1111 WOS Scopus РИНЦ CAPlusCA OpenAlex
Small-Angle X-Ray Characterization of the Nucleoprotein Complexes Resulting from DNA-Induced Oligomerization of HIV-1 Integrase
Nucleic Acids Research. 2007. V.35. N3. P.975-987. DOI: 10.1093/nar/gkl1111 WOS Scopus РИНЦ CAPlusCA OpenAlex
Файлы:
Полный текст от издателя
Даты:
Поступила в редакцию: | 9 окт. 2006 г. |
Принята к публикации: | 28 дек. 2006 г. |
Опубликована online: | 26 янв. 2007 г. |
Опубликована в печати: | 1 февр. 2007 г. |
Идентификаторы БД:
Web of science: | WOS:000244429800031 |
Scopus: | 2-s2.0-33847346415 |
РИНЦ: | 13534672 |
Chemical Abstracts: | 2007:191585 |
Chemical Abstracts (print): | 146:333870 |
OpenAlex: | W2139684940 |