Unknown

Dataset Information

0

P59OASL, a 2'-5' oligoadenylate synthetase like protein: a novel human gene related to the 2'-5' oligoadenylate synthetase family.


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.

SUBMITTER: Hartmann R 

PROVIDER: S-EPMC147837 | biostudies-other | 1998 Sep

REPOSITORIES: biostudies-other

altmetric image

Publications

p59OASL, a 2'-5' oligoadenylate synthetase like protein: a novel human gene related to the 2'-5' oligoadenylate synthetase family.

Hartmann R R   Olsen H S HS   Widder S S   Jorgensen R R   Justesen J J  

Nucleic acids research 19980901 18


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 p  ...[more]

Similar Datasets

| S-EPMC3224142 | biostudies-literature
| S-EPMC1135745 | biostudies-other
| S-EPMC3500226 | biostudies-literature
| S-EPMC8627505 | biostudies-literature
| S-EPMC38217 | biostudies-other
| S-EPMC9215171 | biostudies-literature
| S-EPMC9478401 | biostudies-literature
| S-EPMC4829093 | biostudies-literature
| S-EPMC11275450 | biostudies-literature
| S-EPMC108343 | biostudies-literature