Linked Life Data

9235909

Source:http://linkedlifedata.com/resource/pubmed/id/9235909

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
1997-8-21
pubmed:abstractText
Ribonuclease L (RNase L) is an endoribonuclease that is activated upon binding of adenosine oligomers linked 2' to 5' to cleave viral and cellular RNAs. We recently proposed a model for activation in which activator A binds to monomer, E, to form EA, which subsequently dimerizes to the active form, E2A2 (Cole, J. L., Carroll, S. S., and Kuo, L. C. (1996) J. Biol. Chem. 271, 3978-3981). Here, we have employed this model to define the equilibrium constants for activator binding (Ka) and dimerization of EA to E2A2 (Kd) by equilibrium analytical ultracentrifugation and fluorescence measurements. Multi-wavelength sedimentation data were globally fit to the model above, yielding values of Ka = 1.69 microM and Kd = 17. 8 nM for 2',5'-linked adenosine trimer. Fluorescent conjugates of 2',5'-linked adenosine trimer with 7-hydroxycoumarin have been prepared. The coumarin emission anisotropy shows a large increases upon binding to RNase L. Analysis of anisotropy titrations yields values of Ka and Kd close to those obtained by sedimentation. The sedimentation parameters for unmodified 2',5'-linked adenosine trimer also agree with those obtained by enzyme kinetic methods (Carroll, S. S., Cole, J. L., Viscount, T., Geib, J., Gehman, J., and Kuo, L. C. (1997) J. Biol. Chem. 272, 19193-19198). Thus, the data presented here clearly define the energetics of RNase L activation and support the minimal activation model.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19187-92
pubmed:dateRevised
2011-6-17
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Activation of RNase L by 2',5'-oligoadenylates. Biophysical characterization.
pubmed:affiliation
Department of Antiviral Research, Merck Research Laboratories, West Point, Pennsylvania 19486, USA.
pubmed:publicationType
Journal Article