P59OASL, a 2'-5' Oligoadenylate Synthetase Like Protein: a Novel Human Gene Related to the 2'-5' Oligoadenylate Synthetase Family

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 1998 Sep 2

PMID 9722630

Citations 38

Authors

R Hartmann

H S Olsen

S Widder

R Jorgensen

J Justesen

Affiliations

Soon will be listed here.

Abstract

The 2'-5' oligoadenylate synthetases form a well conserved family of interferon induced proteins, presumably present throughout the mammalian class. Using the Expressed Sequence Tag databases, we have identified a novel member of this family. This protein, which we named p59 2'-5' oligoadenylate synthetase-like protein (p59OASL), shares a highly conserved N-terminal domain with the known forms of 2'-5' oligoadenylate synthetases, but differs completely in its C-terminal part. The C-terminus of p59OASL is formed of two domains of ubiquitin-like sequences. Here we present the characterisation of a full-length cDNA clone, the genomic sequence and the expression pattern of this gene. We have addressed the evolution of the 2'-5' oligoadenylate synthetase gene family, in the light of both this new member and new 2'-5' oligoadenylate synthetase sequence data from other species, which have recently appeared in the databases.

Citing Articles

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Oligoadenylate synthetase 1 displays dual antiviral mechanisms in driving translational shutdown and protecting interferon production.

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The Many Faces of Oligoadenylate Synthetases.

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Pan-cancer analysis identified OAS1 as a potential prognostic biomarker for multiple tumor types.

Jiang S, Deng X, Luo M, Zhou L, Chai J, Tian C Front Oncol. 2023; 13:1207081.

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Occludin Regulates HIV-1 Infection by Modulation of the Interferon Stimulated OAS Gene Family.

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