Source:http://linkedlifedata.com/resource/pubmed/id/15288950
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
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| pubmed:dateCreated |
2004-8-3
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| pubmed:abstractText |
Using an RT-PCR approach a cDNA clone, designated Ms-Rac4 and putatively coding for a small GTPase was isolated from Medicago sativa. Ms-Rac4 and the earlier described Ms-Rac1 [Mol. Gen. Genet. 263 (2000) 761] belong to the class of GTP-binding Rho of plants (Rop) proteins. At the amino acid level they display all conserved regions that are common to GTP-binding proteins. Phylogenetically both are located in the group Ia, but within this group they are well-separated. Computed structure models of both proteins revealed a high degree of structural conservation. Particularly the switch I and switch II region are 100% conserved between Ms-Rac1 and Ms-Rac4 and highly conserved as compared to other Rac-like G-proteins. Both GTPases differ in structure within the fourth loop and the fourth helix. GTP-binding properties of the heterologously expressed Ms-Rac1 and Ms-Rac4 was shown by fluorescence resonance energy transfer (FRET) using mantGTP and by surface plasmon resonance (SPR). By this method the specificity of the G-protein/GTP interaction was shown and the inhibitory effect of GTP, EDTA and Mg(2+) on the Ms-Rac1 and Ms-Rac4 binding to immobilized GTP was characterized. Ms-Rac1 and Ms-Rac4 exhibited the same affinity to GTP and are similarly affected by GTP, EDTA and Mg(2+). Thus, the predicted structural differences do not result in different GTP-binding properties of Ms-Rac1 and Ms-Rac4.
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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/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rac1 GTP-Binding Protein
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| pubmed:status |
MEDLINE
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| pubmed:month |
Aug
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| pubmed:issn |
0168-1656
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
26
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| pubmed:volume |
112
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
151-64
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:15288950-Amino Acid Sequence,
pubmed-meshheading:15288950-Binding Sites,
pubmed-meshheading:15288950-Computer Simulation,
pubmed-meshheading:15288950-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:15288950-GTP Phosphohydrolases,
pubmed-meshheading:15288950-GTP-Binding Proteins,
pubmed-meshheading:15288950-Guanosine Triphosphate,
pubmed-meshheading:15288950-Models, Chemical,
pubmed-meshheading:15288950-Models, Molecular,
pubmed-meshheading:15288950-Molecular Sequence Data,
pubmed-meshheading:15288950-Multiprotein Complexes,
pubmed-meshheading:15288950-Plant Proteins,
pubmed-meshheading:15288950-Protein Binding,
pubmed-meshheading:15288950-Protein Conformation,
pubmed-meshheading:15288950-Protein Interaction Mapping,
pubmed-meshheading:15288950-Sequence Homology, Amino Acid,
pubmed-meshheading:15288950-Structure-Activity Relationship,
pubmed-meshheading:15288950-Surface Plasmon Resonance,
pubmed-meshheading:15288950-rac1 GTP-Binding Protein
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| pubmed:year |
2004
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| pubmed:articleTitle |
The use of surface plasmon resonance (SPR) and fluorescence resonance energy transfer (FRET) to monitor the interaction of the plant G-proteins Ms-Rac1 and Ms-Rac4 with GTP.
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| pubmed:affiliation |
Faculty of Biology, Genetics, University of Bielefeld, D-33501 Bielefeld, Germany.
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't,
Evaluation Studies
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