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


ABSTRACT: 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.

SUBMITTER: Koga R 

PROVIDER: S-EPMC5757179 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

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

Koga Ryoko R   Yamamoto Minami M   Ciftci Halil Ibrahim HI   Otsuka Masami M   Fujita Mikako M  

FEBS open bio 20171219 1


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 li  ...[more]

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