Source:http://linkedlifedata.com/resource/pubmed/id/11689059
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
2001-11-5
|
pubmed:abstractText |
The RNA-specific adenosine deaminase (ADAR1) is an interferon-inducible editing enzyme that converts adenosine to inosine. ADAR1 contains three distinct domains: a N-terminal Z-DNA binding domain that includes two Z-DNA binding motifs; a central double-stranded RNA binding domain that includes three dsRNA binding motifs (dsRBM); and a C-terminal catalytic domain responsible for A-to-I enzymatic activity. The E3L protein of vaccinia virus mediates interferon resistance. E3L, similar to ADAR1, also contains Z-DNA binding and dsRNA binding motifs. To assess the possible role of E3L in modulating RNA editing by ADAR1, we examined the effect of E3L on ADAR1 deaminase activity. Wild-type E3L protein was a potent inhibitor of ADAR1 deaminase enzymatic activity. Analysis of mutant E3L proteins indicated that the carboxy-proximal dsRBM of E3L was essential for antagonism of ADAR1. Surprisingly, disruption of the Z-DNA binding domain of E3L by double substitutions of two highly conserved residues also abolished its antagonistic activity, whereas deletion of the entire Z domain had little effect on the inhibition. With natural neurotransmitter pre-mRNA substrates, E3L weakly inhibited the site-selective editing activity by ADAR1 at the R/G site of the glutamate receptor B subunit (GluR-B) pre-mRNA and the A site of serotonin 2C receptor (5-HT2CR) pre-mRNA; editing of the intronic hotspot (+)60 site of GluR-B was not affected by E3L. These results demonstrate that the A-to-I RNA editing activity of the IFN-inducible adenosine deaminase is impaired by the product of the vaccinia virus E3L interferon resistance gene.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Deaminase,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Deaminase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/E3L protein, Vaccinia virus,
http://linkedlifedata.com/resource/pubmed/chemical/Inosine,
http://linkedlifedata.com/resource/pubmed/chemical/Interferons,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/dsRNA adenosine deaminase
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0042-6822
|
pubmed:author | |
pubmed:copyrightInfo |
Copyright 2001 Academic Press.
|
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
289
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
378-87
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:11689059-Adenosine,
pubmed-meshheading:11689059-Adenosine Deaminase,
pubmed-meshheading:11689059-Adenosine Deaminase Inhibitors,
pubmed-meshheading:11689059-Inosine,
pubmed-meshheading:11689059-Interferons,
pubmed-meshheading:11689059-Mutation,
pubmed-meshheading:11689059-RNA Editing,
pubmed-meshheading:11689059-RNA-Binding Proteins,
pubmed-meshheading:11689059-Vaccinia virus,
pubmed-meshheading:11689059-Viral Proteins
|
pubmed:year |
2001
|
pubmed:articleTitle |
Vaccinia virus E3L interferon resistance protein inhibits the interferon-induced adenosine deaminase A-to-I editing activity.
|
pubmed:affiliation |
Department of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, California 93106, USA.
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|