Nucleic Acids Research Advance Access originally published online on January 26, 2007
Nucleic Acids Research 2007 35(3):975-987; doi:10.1093/nar/gkl1111
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Nucleic Acids Research, 2007, Vol. 35, No. 3 975-987
© 2007 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Structural Biology |
Small-angle X-ray characterization of the nucleoprotein complexes resulting from DNA-induced oligomerization of HIV-1 integrase
1Institute of Chemical Biology and Fundamental Medicine, Siberian Division of Russian Academy of Sciences. Lavrentieva Ave. 8, 630090, Russia; 2Institute of Catalysis, Siberian Division of Russian Academy of Sciences. Lavrentyeva Ave. 3, 630090, Russia and 3UMR 5097 CNRS-Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux cedex, France and IFR 66 Bordeaux, France
*To whom correspondence should be addressed. Tel: 7-383-3356226; Fax: 7-383- 333 36 77; E-mail: nevinsky{at}niboch.nsc.ru. Correspondence may also be addressed to Vincent Parissi. Tel: 33-5 5757 1740; Fax: 33-5 5757 1766; E-mail: vincent.parissi{at}reger.u-bordeaux2.fr
Received October 9, 2006. Revised November 28, 2006. Accepted December 28, 2006.
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 (Rg), 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.
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