Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G

APOBEC3G inhibits HIV-1 viral replication via catalytic and non-catalytic processes. Here the authors show that APOBEC3G binds single-stranded DNA as an active deaminase monomer, subsequently forming catalytic-inactive dimers that block reverse transcriptase-mediated DNA synthesis.

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Autores principales:	Michael Morse, Ran Huo, Yuqing Feng, Ioulia Rouzina, Linda Chelico, Mark C. Williams
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b9af9a0b30144b59809406b814538401
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spelling	oai:doaj.org-article:b9af9a0b30144b59809406b8145384012021-12-02T14:40:34ZDimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G10.1038/s41467-017-00501-y2041-1723https://doaj.org/article/b9af9a0b30144b59809406b8145384012017-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00501-yhttps://doaj.org/toc/2041-1723APOBEC3G inhibits HIV-1 viral replication via catalytic and non-catalytic processes. Here the authors show that APOBEC3G binds single-stranded DNA as an active deaminase monomer, subsequently forming catalytic-inactive dimers that block reverse transcriptase-mediated DNA synthesis.Michael MorseRan HuoYuqing FengIoulia RouzinaLinda ChelicoMark C. WilliamsNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Michael Morse Ran Huo Yuqing Feng Ioulia Rouzina Linda Chelico Mark C. Williams Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G
description	APOBEC3G inhibits HIV-1 viral replication via catalytic and non-catalytic processes. Here the authors show that APOBEC3G binds single-stranded DNA as an active deaminase monomer, subsequently forming catalytic-inactive dimers that block reverse transcriptase-mediated DNA synthesis.
format	article
author	Michael Morse Ran Huo Yuqing Feng Ioulia Rouzina Linda Chelico Mark C. Williams
author_facet	Michael Morse Ran Huo Yuqing Feng Ioulia Rouzina Linda Chelico Mark C. Williams
author_sort	Michael Morse
title	Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G
title_short	Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G
title_full	Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G
title_fullStr	Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G
title_full_unstemmed	Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G
title_sort	dimerization regulates both deaminase-dependent and deaminase-independent hiv-1 restriction by apobec3g
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/b9af9a0b30144b59809406b814538401
work_keys_str_mv	AT michaelmorse dimerizationregulatesbothdeaminasedependentanddeaminaseindependenthiv1restrictionbyapobec3g AT ranhuo dimerizationregulatesbothdeaminasedependentanddeaminaseindependenthiv1restrictionbyapobec3g AT yuqingfeng dimerizationregulatesbothdeaminasedependentanddeaminaseindependenthiv1restrictionbyapobec3g AT iouliarouzina dimerizationregulatesbothdeaminasedependentanddeaminaseindependenthiv1restrictionbyapobec3g AT lindachelico dimerizationregulatesbothdeaminasedependentanddeaminaseindependenthiv1restrictionbyapobec3g AT markcwilliams dimerizationregulatesbothdeaminasedependentanddeaminaseindependenthiv1restrictionbyapobec3g
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Dimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3G

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