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Small-angle X-ray characterization of the nucleoprotein complexes resulting from DNA-induced oligomerization of HIV-1 integrase
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 specificit...
Autores principales: | , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1807944/ https://www.ncbi.nlm.nih.gov/pubmed/17259219 http://dx.doi.org/10.1093/nar/gkl1111 |
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author | Baranova, Svetlana Tuzikov, Fedor V. Zakharova, Olga D. Tuzikova, Natalia A. Calmels, Christina Litvak, Simon Tarrago-Litvak, Laura Parissi, Vincent Nevinsky, Georgy A. |
author_facet | Baranova, Svetlana Tuzikov, Fedor V. Zakharova, Olga D. Tuzikova, Natalia A. Calmels, Christina Litvak, Simon Tarrago-Litvak, Laura Parissi, Vincent Nevinsky, Georgy A. |
author_sort | Baranova, Svetlana |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-1807944 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-18079442007-03-02 Small-angle X-ray characterization of the nucleoprotein complexes resulting from DNA-induced oligomerization of HIV-1 integrase Baranova, Svetlana Tuzikov, Fedor V. Zakharova, Olga D. Tuzikova, Natalia A. Calmels, Christina Litvak, Simon Tarrago-Litvak, Laura Parissi, Vincent Nevinsky, Georgy A. Nucleic Acids Res Structural Biology 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. Oxford University Press 2007-02 2007-01-26 /pmc/articles/PMC1807944/ /pubmed/17259219 http://dx.doi.org/10.1093/nar/gkl1111 Text en © 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. |
spellingShingle | Structural Biology Baranova, Svetlana Tuzikov, Fedor V. Zakharova, Olga D. Tuzikova, Natalia A. Calmels, Christina Litvak, Simon Tarrago-Litvak, Laura Parissi, Vincent Nevinsky, Georgy A. Small-angle X-ray characterization of the nucleoprotein complexes resulting from DNA-induced oligomerization of HIV-1 integrase |
title | Small-angle X-ray characterization of the nucleoprotein complexes resulting from DNA-induced oligomerization of HIV-1 integrase |
title_full | Small-angle X-ray characterization of the nucleoprotein complexes resulting from DNA-induced oligomerization of HIV-1 integrase |
title_fullStr | Small-angle X-ray characterization of the nucleoprotein complexes resulting from DNA-induced oligomerization of HIV-1 integrase |
title_full_unstemmed | Small-angle X-ray characterization of the nucleoprotein complexes resulting from DNA-induced oligomerization of HIV-1 integrase |
title_short | Small-angle X-ray characterization of the nucleoprotein complexes resulting from DNA-induced oligomerization of HIV-1 integrase |
title_sort | small-angle x-ray characterization of the nucleoprotein complexes resulting from dna-induced oligomerization of hiv-1 integrase |
topic | Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1807944/ https://www.ncbi.nlm.nih.gov/pubmed/17259219 http://dx.doi.org/10.1093/nar/gkl1111 |
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