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

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.

Bibliographic Details
Main Authors: Michael Morse, Ran Huo, Yuqing Feng, Ioulia Rouzina, Linda Chelico, Mark C. Williams
Format: Article
Language:English
Published: Nature Publishing Group 2017-09-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-017-00501-y
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spelling doaj-b9af9a0b30144b59809406b8145384012021-05-11T07:21:03ZengNature Publishing GroupNature Communications2041-17232017-09-018111110.1038/s41467-017-00501-yDimerization regulates both deaminase-dependent and deaminase-independent HIV-1 restriction by APOBEC3GMichael Morse0Ran Huo1Yuqing Feng2Ioulia Rouzina3Linda Chelico4Mark C. Williams5Department of Physics, Northeastern UniversityDepartment of Physics, Northeastern UniversityDepartment of Microbiology and Immunology, University of SaskatchewanDepartment of Chemistry and Biochemistry, Ohio State UniversityDepartment of Microbiology and Immunology, University of SaskatchewanDepartment of Physics, Northeastern UniversityAPOBEC3G 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.https://doi.org/10.1038/s41467-017-00501-y
collection DOAJ
language English
format Article
sources DOAJ
author Michael Morse
Ran Huo
Yuqing Feng
Ioulia Rouzina
Linda Chelico
Mark C. Williams
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-09-01
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.
url https://doi.org/10.1038/s41467-017-00501-y
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AT yuqingfeng dimerizationregulatesbothdeaminasedependentanddeaminaseindependenthiv1restrictionbyapobec3g
AT iouliarouzina dimerizationregulatesbothdeaminasedependentanddeaminaseindependenthiv1restrictionbyapobec3g
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