Linked Life Data

9346316

Source:http://linkedlifedata.com/resource/pubmed/id/9346316

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-11-21
pubmed:abstractText
The (2'-5')oligoadenylate synthetase represents a family of interferon-induced proteins which when activated by double-stranded (ds)RNA polymerizes ATP into 2'-5'-linked oligomers with the general formula pppA(2'p5'A)n, where n > 1, which for convenience are referred to as 2-5A. We studied here the influence of pH, dsRNA concentration and time on oligomeric composition of 2-5A synthesized by purified 69-kDa and 100-kDa isoforms of (2'-5')oligo(adenylate) synthetase. In optimal conditions for activity, the 69-kDa form synthesized higher oligomers of 2-5A molecules whereas the 100 kDa form synthesized preferentially dimeric molecules, which are known not to be functional for the activation of RNase L. This difference does not reflect a differential affinity of the enzymes for the preformed 2-5A dimer, which is found to be a very poor substrate for both enzymes. This latter strongly suggests that the mechanism of elongation is more likely processive. Moreover, we show that both isoforms have efficient nucleotidyl-transferase activity and provide evidence that, in optimized conditions, GTP can be used alone as substrate by these enzymes to generate pppG2'p5'G. Our results clearly demonstrate that the 69-kDa and 100-kDa forms of (2'-5')oligoadenylate synthetase manifest various differential catalytic activities, and favor the hypothesis that these enzymes might have other functions in the cell besides those in the 2-5A system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
248
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
558-66
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
69-kDa and 100-kDa isoforms of interferon-induced (2'-5')oligoadenylate synthetase exhibit differential catalytic parameters.
pubmed:affiliation
Unité de Virologie et Immunologie Cellulaire (ERS CNRS 572) Institut Pasteur, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't