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.
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2017-09-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-017-00501-y |
| _version_ | 1818857754803044352 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-12-19T08:45:25Z |
| format | Article |
| id | doaj.art-b9af9a0b30144b59809406b814538401 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-19T08:45:25Z |
| publishDate | 2017-09-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-b9af9a0b30144b59809406b8145384012022-12-21T20:28:49ZengNature PortfolioNature 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 |
| 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 |
| title | 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_short | 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 |
| url | https://doi.org/10.1038/s41467-017-00501-y |
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