Small-Angle X-Ray Characterization of the Nucleoprotein Complexes Resulting from DNA-Induced Oligomerization of HIV-1 Integrase | Sciact - CRIS-system of Boreskov Institute of Catalysis

Small-Angle X-Ray Characterization of the Nucleoprotein Complexes Resulting from DNA-Induced Oligomerization of HIV-1 Integrase Full article

Journal

Nucleic Acids Research
ISSN: 0305-1048 , E-ISSN: 1362-4962

Output data

Year: 2007, Volume: 35, Number: 3, Pages: 975-987 Pages count : 13 DOI: 10.1093/nar/gkl1111

Tags

IMMUNODEFICIENCY-VIRUS TYPE-1; RESOLVED FLUORESCENCE ANISOTROPY; CARBOXYL-TERMINAL DOMAINS; VIRAL-DNA; CRYSTAL-STRUCTURE; RETROVIRAL DNA; BINDING; PROTEIN; CORE; MULTIMERIZATION

Authors

Baranova Svetlana ¹ , Tuzikov Fedor V. ² , Zakharova Olga D. ¹ , Tuzikova Natalia A. ² , Calmels Christina ³ , Litvak Simon ³ , Tarrago-Litvak Laura ³ , Parissi Vincent ³ , Nevinsky Georgy A. ¹

Affiliations

1	Institute of Chemical Biology and Fundamental Medicine, Siberian Division of Russian Academy of Sciences, Lavrentieva Ave. 8, 630090, Russia
2	Institute of Catalysis, Siberian Division of Russian Academy of Sciences, Lavrentyeva Ave. 3, 630090, Russia
3	UMR 5097 CNRS-Universite Victor Segalen Bordeaux 2, 146 rue Leo Saignat, 33076 Bordeaux cedex, France and IFR 66 Bordeaux, France

Funding (6)

1	Russian Foundation for Basic Research	03-04-49781
2	Siberian Branch of the Russian Academy of Sciences
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

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.

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 ANCAN OpenAlex

Full text from publisher

Submitted:	Oct 9, 2006
Accepted:	Dec 28, 2006
Published online:	Jan 26, 2007
Published print:	Feb 1, 2007

Web of science:	WOS:000244429800031
Scopus:	2-s2.0-33847346415
Elibrary:	13534672
Chemical Abstracts:	2007:191585
Chemical Abstracts (print):	146:333870
OpenAlex:	W2139684940

DB	Citing
Web of science	19
Scopus	19
Elibrary	20
OpenAlex	24