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J Biol Chem, Vol. 274, Issue 3, 1557-1565, January 15, 1999
From the The 2-5A synthetases represent a family of
proteins implicated in the mechanism of the antiviral action of
interferon. When activated by double-stranded RNA, these proteins
polymerize ATP into 2'-5'-linked oligomers with the general formula
pppA(2'p5'A)n, n
The 100-kDa 2',5'-Oligoadenylate Synthetase Catalyzing
Preferentially the Synthesis of Dimeric pppA2'p5'A Molecules Is
Composed of Three Homologous Domains
,, and
Unité de Virologie et Imunologie
Cellulaire, ERS CNRS 572, Institut Pasteur, 75724 Paris Cédex 15, France and the § Wellcome Trust Centre for Human Genetics,
University of Oxford, Oxford OX1 2JD, United Kingdom
1. Three
forms of human 2-5A synthetases have been described corresponding to
proteins of 40/46 (p40/p46), 69/71 (p69/p71), and 100 kDa (p100). Here
we describe the molecular cloning and characterization of p100. By
screening a cDNA expression library with a specific p100 polyclonal
antibody, we first isolated a 590-nucleotide cDNA fragment which
was subsequently used to isolate the full-length 6365-nucleotide
cDNA. This cDNA recognizes a distinct interferon-induced
messenger RNA of 7 kilobases. It has an open reading frame encoding a
protein of 1087 amino acids including the sequence of seven peptides
obtained by microsequencing of the natural p100 protein, which was
purified from interferon-treated human cells. p100 is composed of three
adjacent domains, each homologous to the previously defined catalytic
unit of 350 amino acids, which is present as one unit in p40/p46 and as
two units in p69/p71. The recombinant p100 synthesized preferentially
dimeric 2',5'-oligoadenylate molecules and displayed parameters for
maximum enzyme activity similar to the natural p100. These results
confirm that the enzymatic activity of p100 is distinct compared with that of p40/p46 and p69/p71.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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