Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1999-2-11
|
| pubmed:databankReference | |
| pubmed:abstractText |
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 >/= 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2',5'-Oligoadenylate Synthetase,
http://linkedlifedata.com/resource/pubmed/chemical/Adenine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Oligoribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/adenosine triphosphate adenosine...
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
274
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1557-65
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9880533-2',5'-Oligoadenylate Synthetase,
pubmed-meshheading:9880533-Adenine Nucleotides,
pubmed-meshheading:9880533-Blotting, Northern,
pubmed-meshheading:9880533-Catalysis,
pubmed-meshheading:9880533-DNA, Complementary,
pubmed-meshheading:9880533-Dimerization,
pubmed-meshheading:9880533-Fluorescent Dyes,
pubmed-meshheading:9880533-HeLa Cells,
pubmed-meshheading:9880533-Humans,
pubmed-meshheading:9880533-Hydrogen-Ion Concentration,
pubmed-meshheading:9880533-Interferon-alpha,
pubmed-meshheading:9880533-Molecular Sequence Data,
pubmed-meshheading:9880533-Molecular Weight,
pubmed-meshheading:9880533-Oligoribonucleotides,
pubmed-meshheading:9880533-Open Reading Frames,
pubmed-meshheading:9880533-RNA, Double-Stranded,
pubmed-meshheading:9880533-Recombinant Proteins,
pubmed-meshheading:9880533-Sequence Homology, Amino Acid,
pubmed-meshheading:9880533-Transfection
|
| pubmed:year |
1999
|
| pubmed:articleTitle |
The 100-kDa 2',5'-oligoadenylate synthetase catalyzing preferentially the synthesis of dimeric pppA2'p5'A molecules is composed of three homologous domains.
|
| pubmed:affiliation |
Unité de Virologie et Imunologie Cellulaire, ERS CNRS 572, Institut Pasteur, 75724 Paris Cédex 15, France.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|