Cargando…
Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase
Reverse transcription describes the process of the transformation of single-stranded RNA into double-stranded DNA via an RNA/DNA duplex intermediate, and is catalyzed by the viral enzyme reverse transcriptase (RT). This event is a pivotal step in the life cycle of all retroviruses. In contrast to or...
Autor principal: | |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6669543/ https://www.ncbi.nlm.nih.gov/pubmed/31269675 http://dx.doi.org/10.3390/v11070598 |
_version_ | 1783440395434196992 |
---|---|
author | Wöhrl, Birgitta M. |
author_facet | Wöhrl, Birgitta M. |
author_sort | Wöhrl, Birgitta M. |
collection | PubMed |
description | Reverse transcription describes the process of the transformation of single-stranded RNA into double-stranded DNA via an RNA/DNA duplex intermediate, and is catalyzed by the viral enzyme reverse transcriptase (RT). This event is a pivotal step in the life cycle of all retroviruses. In contrast to orthoretroviruses, the domain structure of the mature RT of foamy viruses is different, i.e., it harbors the protease (PR) domain at its N-terminus, thus being a PR-RT. This structural feature has consequences on PR activation, since the enzyme is monomeric in solution and retroviral PRs are only active as dimers. This review focuses on the structural and functional aspects of simian and prototype foamy virus reverse transcription and reverse transcriptase, as well as special features of reverse transcription that deviate from orthoretroviral processes, e.g., PR activation. |
format | Online Article Text |
id | pubmed-6669543 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-66695432019-08-08 Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase Wöhrl, Birgitta M. Viruses Review Reverse transcription describes the process of the transformation of single-stranded RNA into double-stranded DNA via an RNA/DNA duplex intermediate, and is catalyzed by the viral enzyme reverse transcriptase (RT). This event is a pivotal step in the life cycle of all retroviruses. In contrast to orthoretroviruses, the domain structure of the mature RT of foamy viruses is different, i.e., it harbors the protease (PR) domain at its N-terminus, thus being a PR-RT. This structural feature has consequences on PR activation, since the enzyme is monomeric in solution and retroviral PRs are only active as dimers. This review focuses on the structural and functional aspects of simian and prototype foamy virus reverse transcription and reverse transcriptase, as well as special features of reverse transcription that deviate from orthoretroviral processes, e.g., PR activation. MDPI 2019-07-02 /pmc/articles/PMC6669543/ /pubmed/31269675 http://dx.doi.org/10.3390/v11070598 Text en © 2019 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Wöhrl, Birgitta M. Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase |
title | Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase |
title_full | Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase |
title_fullStr | Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase |
title_full_unstemmed | Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase |
title_short | Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase |
title_sort | structural and functional aspects of foamy virus protease-reverse transcriptase |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6669543/ https://www.ncbi.nlm.nih.gov/pubmed/31269675 http://dx.doi.org/10.3390/v11070598 |
work_keys_str_mv | AT wohrlbirgittam structuralandfunctionalaspectsoffoamyvirusproteasereversetranscriptase |