Source:http://linkedlifedata.com/resource/pubmed/id/19470518
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2009-8-27
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pubmed:abstractText |
The interactions of recombinant human eIF4A (4A) and its N- and C-terminal side domains (AN and AC, respectively) with the middle- and C-terminal-domain-linked fragment (GMC) of eIF4G and its middle and C-terminal domains (GM and GC, respectively) were investigated by surface plasmon resonance (SPR) analysis and isothermal titration calorimetry (ITC). It is remarkable that the kinetic parameter-dependent SPR profile observed for the 4A-GMC pair was quite different from the steady affinity profiles of the 4A-GM/GC pairs, suggesting the simultaneous contribution of the middle and C-terminal domains of eIF4G for the binding with eIF4A. On the other hand, ITC yielded the enthalpy energies of -1.5 x 10(4) to -2.5 x 10(4) J/mol for the domain-domain interactions of 4A with GMC. Although the ITC profile of the 4A-GM pair reflects well the structural feature shown previously by NMR and X-ray analyses, it was essentially different from that of the 4A-GMC pair. The present results suggest that the intimate interaction between the eIF4A N- and C-terminal domains and the eIF4G middle and C-terminal domains is necessary to reveal the biologically active function of the eIF4A-eIF4G complex.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/EIF4G1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-4A,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-4G,
http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1756-2651
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
146
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
359-68
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pubmed:meshHeading |
pubmed-meshheading:19470518-Calorimetry,
pubmed-meshheading:19470518-Eukaryotic Initiation Factor-4A,
pubmed-meshheading:19470518-Eukaryotic Initiation Factor-4G,
pubmed-meshheading:19470518-Humans,
pubmed-meshheading:19470518-Kinetics,
pubmed-meshheading:19470518-Models, Molecular,
pubmed-meshheading:19470518-Mutant Proteins,
pubmed-meshheading:19470518-Protein Interaction Domains and Motifs,
pubmed-meshheading:19470518-Protein Multimerization,
pubmed-meshheading:19470518-Recombinant Fusion Proteins,
pubmed-meshheading:19470518-Surface Plasmon Resonance,
pubmed-meshheading:19470518-Thermodynamics,
pubmed-meshheading:19470518-Titrimetry,
pubmed-meshheading:19470518-Transition Temperature
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pubmed:year |
2009
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pubmed:articleTitle |
Domain-dependent interaction of eukaryotic initiation factor eIF4A for binding to middle and C-terminal domains of eIF4G.
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pubmed:affiliation |
Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, 4-20-1 Nasahara, Takatsuki, Osaka 569-1094, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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