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Introduction of H2C2‐type zinc‐binding residues into HIV‐2 Vpr increases its expression level

Human immunodeficiency virus type 2 has two structurally similar proteins, Vpx and Vpr. Vpx degrades the host anti‐viral protein SAMHD1 and is expressed at high levels, while Vpr is responsible for cell cycle arrest and is expressed at much lower levels. We constructed a Vpr mutant with a high level...

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Autores principales: Koga, Ryoko, Yamamoto, Minami, Ciftci, Halil Ibrahim, Otsuka, Masami, Fujita, Mikako
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5757179/
https://www.ncbi.nlm.nih.gov/pubmed/29321964
http://dx.doi.org/10.1002/2211-5463.12358
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author Koga, Ryoko
Yamamoto, Minami
Ciftci, Halil Ibrahim
Otsuka, Masami
Fujita, Mikako
author_facet Koga, Ryoko
Yamamoto, Minami
Ciftci, Halil Ibrahim
Otsuka, Masami
Fujita, Mikako
author_sort Koga, Ryoko
collection PubMed
description Human immunodeficiency virus type 2 has two structurally similar proteins, Vpx and Vpr. Vpx degrades the host anti‐viral protein SAMHD1 and is expressed at high levels, while Vpr is responsible for cell cycle arrest and is expressed at much lower levels. We constructed a Vpr mutant with a high level of expression by replacing the amino acids HHCR/HHCH with a putative H2C2‐type zinc‐binding site that is carried by Vpx. Our finding suggests that during the evolution of Vpr and Vpx, zinc‐binding likely became a mechanism for regulating their expression levels.
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spelling pubmed-57571792018-01-10 Introduction of H2C2‐type zinc‐binding residues into HIV‐2 Vpr increases its expression level Koga, Ryoko Yamamoto, Minami Ciftci, Halil Ibrahim Otsuka, Masami Fujita, Mikako FEBS Open Bio Research Articles Human immunodeficiency virus type 2 has two structurally similar proteins, Vpx and Vpr. Vpx degrades the host anti‐viral protein SAMHD1 and is expressed at high levels, while Vpr is responsible for cell cycle arrest and is expressed at much lower levels. We constructed a Vpr mutant with a high level of expression by replacing the amino acids HHCR/HHCH with a putative H2C2‐type zinc‐binding site that is carried by Vpx. Our finding suggests that during the evolution of Vpr and Vpx, zinc‐binding likely became a mechanism for regulating their expression levels. John Wiley and Sons Inc. 2017-12-19 /pmc/articles/PMC5757179/ /pubmed/29321964 http://dx.doi.org/10.1002/2211-5463.12358 Text en © 2017 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Koga, Ryoko
Yamamoto, Minami
Ciftci, Halil Ibrahim
Otsuka, Masami
Fujita, Mikako
Introduction of H2C2‐type zinc‐binding residues into HIV‐2 Vpr increases its expression level
title Introduction of H2C2‐type zinc‐binding residues into HIV‐2 Vpr increases its expression level
title_full Introduction of H2C2‐type zinc‐binding residues into HIV‐2 Vpr increases its expression level
title_fullStr Introduction of H2C2‐type zinc‐binding residues into HIV‐2 Vpr increases its expression level
title_full_unstemmed Introduction of H2C2‐type zinc‐binding residues into HIV‐2 Vpr increases its expression level
title_short Introduction of H2C2‐type zinc‐binding residues into HIV‐2 Vpr increases its expression level
title_sort introduction of h2c2‐type zinc‐binding residues into hiv‐2 vpr increases its expression level
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5757179/
https://www.ncbi.nlm.nih.gov/pubmed/29321964
http://dx.doi.org/10.1002/2211-5463.12358
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