Source:http://linkedlifedata.com/resource/pubmed/id/10329541
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1999-6-15
|
pubmed:abstractText |
The 2'-5' oligoadenylate synthetases and the protein kinase PKR are both interferon-induced, double-stranded RNA-dependent proteins that play important roles in the antiviral effects of the interferons and in cellular growth control. Both enzymes are activated by natural or synthetic dsRNAs and by single-stranded RNAs that possess extensive secondary structure. This report describes the effects of the small Epstein-Barr virus-encoded RNA EBER-1 on the regulation of 2-5(A) synthetase activity. We demonstrate that EBER-1 RNA binds to and activates the human 40-kDa 2-5(A) synthetase in a dose-dependent manner. The efficiency of EBER-1 as an activator of 2-5(A) synthetase is approximately 25% of that of the synthetic double-stranded RNA poly(I)/poly(C), and poly(I)/poly(C) further stimulates enzyme activity even in the presence of a high concentration of EBER-1. Conversely, EBER-1 neither stimulates nor inhibits 2-5(A) synthetase that has been activated by a high concentration of poly(I)/poly(C). Competitive binding assays suggest that the relative affinity of the enzyme for poly(I)/poly(C) is considerably higher than that for EBER-1. Our data indicate that EBER-1, like VAI RNA of adenovirus, TAR RNA of HIV-1, and Rex-RE RNA of HTLV-1, is able to activate the 2-5(A) synthetases. The significance of why several viruses may activate the 2-5(A) synthetase/RNase L-mediated RNA degradation pathway is discussed.
|
pubmed:grant | |
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/Epstein-Barr virus encoded RNA 1,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon Inducers,
http://linkedlifedata.com/resource/pubmed/chemical/Interferons,
http://linkedlifedata.com/resource/pubmed/chemical/Poly I-C,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0042-6822
|
pubmed:author | |
pubmed:copyrightInfo |
Copyright 1999 Academic Press.
|
pubmed:issnType |
Print
|
pubmed:day |
10
|
pubmed:volume |
257
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
303-13
|
pubmed:dateRevised |
2009-9-29
|
pubmed:meshHeading |
pubmed-meshheading:10329541-2',5'-Oligoadenylate Synthetase,
pubmed-meshheading:10329541-Animals,
pubmed-meshheading:10329541-Cell Line,
pubmed-meshheading:10329541-Enzyme Activation,
pubmed-meshheading:10329541-Herpesvirus 4, Human,
pubmed-meshheading:10329541-Humans,
pubmed-meshheading:10329541-Interferon Inducers,
pubmed-meshheading:10329541-Interferons,
pubmed-meshheading:10329541-Poly I-C,
pubmed-meshheading:10329541-RNA, Viral,
pubmed-meshheading:10329541-Recombinant Fusion Proteins,
pubmed-meshheading:10329541-Spodoptera
|
pubmed:year |
1999
|
pubmed:articleTitle |
Activation of the interferon-inducible (2'-5') oligoadenylate synthetase by the Epstein-Barr virus RNA, EBER-1.
|
pubmed:affiliation |
Cellular and Molecular Sciences Group, St. George's Hospital Medical School, Cranmer Terrace, London, SW17 0RE, United Kingdom.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|