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Prototype foamy virus integrase is promiscuous for target choice
Retroviruses have two essential activities: reverse transcription and integration. The viral protein integrase (IN) covalently joins the viral cDNA genome to the host DNA. Prototype foamy virus (PFV) IN has become a model of retroviral intasome structure. However, this retroviral IN has not been wel...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6119477/ https://www.ncbi.nlm.nih.gov/pubmed/30017200 http://dx.doi.org/10.1016/j.bbrc.2018.07.031 |
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author | Mackler, R.M. Lopez, M.A. Osterhage, M.J. Yoder, K.E. |
author_facet | Mackler, R.M. Lopez, M.A. Osterhage, M.J. Yoder, K.E. |
author_sort | Mackler, R.M. |
collection | PubMed |
description | Retroviruses have two essential activities: reverse transcription and integration. The viral protein integrase (IN) covalently joins the viral cDNA genome to the host DNA. Prototype foamy virus (PFV) IN has become a model of retroviral intasome structure. However, this retroviral IN has not been well-characterized biochemically. Here we compare PFV IN to previously reported HIV-1 IN activities and discover significant differences. PFV IN is able to utilize the divalent cation calcium during strand transfer while HIV-1 IN is not. HIV-1 IN was shown to completely commit to a target DNA within 1 min, while PFV IN is not fully committed after 60 min. These results suggest that PFV IN is more promiscuous compared to HIV-1 IN in terms of divalent cation and target commitment. |
format | Online Article Text |
id | pubmed-6119477 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
record_format | MEDLINE/PubMed |
spelling | pubmed-61194772018-09-10 Prototype foamy virus integrase is promiscuous for target choice Mackler, R.M. Lopez, M.A. Osterhage, M.J. Yoder, K.E. Biochem Biophys Res Commun Article Retroviruses have two essential activities: reverse transcription and integration. The viral protein integrase (IN) covalently joins the viral cDNA genome to the host DNA. Prototype foamy virus (PFV) IN has become a model of retroviral intasome structure. However, this retroviral IN has not been well-characterized biochemically. Here we compare PFV IN to previously reported HIV-1 IN activities and discover significant differences. PFV IN is able to utilize the divalent cation calcium during strand transfer while HIV-1 IN is not. HIV-1 IN was shown to completely commit to a target DNA within 1 min, while PFV IN is not fully committed after 60 min. These results suggest that PFV IN is more promiscuous compared to HIV-1 IN in terms of divalent cation and target commitment. 2018-07-14 2018-09-10 /pmc/articles/PMC6119477/ /pubmed/30017200 http://dx.doi.org/10.1016/j.bbrc.2018.07.031 Text en http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Mackler, R.M. Lopez, M.A. Osterhage, M.J. Yoder, K.E. Prototype foamy virus integrase is promiscuous for target choice |
title | Prototype foamy virus integrase is promiscuous for target choice |
title_full | Prototype foamy virus integrase is promiscuous for target choice |
title_fullStr | Prototype foamy virus integrase is promiscuous for target choice |
title_full_unstemmed | Prototype foamy virus integrase is promiscuous for target choice |
title_short | Prototype foamy virus integrase is promiscuous for target choice |
title_sort | prototype foamy virus integrase is promiscuous for target choice |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6119477/ https://www.ncbi.nlm.nih.gov/pubmed/30017200 http://dx.doi.org/10.1016/j.bbrc.2018.07.031 |
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