Structural Basis of the Association of HIV-1 Matrix Protein with DNA

HIV-1 matrix (MA) is a multifunctional protein that is synthesized as a polyprotein that is cleaved by protease during viral maturation. MA contains a cluster of basic residues whose role is controversial. Proposed functions include membrane anchoring, facilitating viral assembly, and directing nucl...

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Detalles Bibliográficos
Autores principales: Cai, Mengli, Huang, Ying, Craigie, Robert, Clore, G. Marius
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2010
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3009736/
https://www.ncbi.nlm.nih.gov/pubmed/21203471
http://dx.doi.org/10.1371/journal.pone.0015675
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author Cai, Mengli
Huang, Ying
Craigie, Robert
Clore, G. Marius
author_facet Cai, Mengli
Huang, Ying
Craigie, Robert
Clore, G. Marius
author_sort Cai, Mengli
collection PubMed
description HIV-1 matrix (MA) is a multifunctional protein that is synthesized as a polyprotein that is cleaved by protease during viral maturation. MA contains a cluster of basic residues whose role is controversial. Proposed functions include membrane anchoring, facilitating viral assembly, and directing nuclear import of the viral DNA. Since MA has been reported to be a component of the preintegration complex (PIC), we have used NMR to probe its interaction with other PIC components. We show that MA interacts with DNA and this is likely sufficient to account for its association with the PIC.
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spelling pubmed-30097362011-01-03 Structural Basis of the Association of HIV-1 Matrix Protein with DNA Cai, Mengli Huang, Ying Craigie, Robert Clore, G. Marius PLoS One Research Article HIV-1 matrix (MA) is a multifunctional protein that is synthesized as a polyprotein that is cleaved by protease during viral maturation. MA contains a cluster of basic residues whose role is controversial. Proposed functions include membrane anchoring, facilitating viral assembly, and directing nuclear import of the viral DNA. Since MA has been reported to be a component of the preintegration complex (PIC), we have used NMR to probe its interaction with other PIC components. We show that MA interacts with DNA and this is likely sufficient to account for its association with the PIC. Public Library of Science 2010-12-23 /pmc/articles/PMC3009736/ /pubmed/21203471 http://dx.doi.org/10.1371/journal.pone.0015675 Text en This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. https://creativecommons.org/publicdomain/zero/1.0/ This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.
spellingShingle Research Article
Cai, Mengli
Huang, Ying
Craigie, Robert
Clore, G. Marius
Structural Basis of the Association of HIV-1 Matrix Protein with DNA
title Structural Basis of the Association of HIV-1 Matrix Protein with DNA
title_full Structural Basis of the Association of HIV-1 Matrix Protein with DNA
title_fullStr Structural Basis of the Association of HIV-1 Matrix Protein with DNA
title_full_unstemmed Structural Basis of the Association of HIV-1 Matrix Protein with DNA
title_short Structural Basis of the Association of HIV-1 Matrix Protein with DNA
title_sort structural basis of the association of hiv-1 matrix protein with dna
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3009736/
https://www.ncbi.nlm.nih.gov/pubmed/21203471
http://dx.doi.org/10.1371/journal.pone.0015675
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AT cloregmarius structuralbasisoftheassociationofhiv1matrixproteinwithdna

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