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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2001-5-25
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pubmed:databankReference |
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pubmed:abstractText |
Rag A/Gtr1p are G proteins and are known to be involved in the RCC1-Ran pathway. We employed the two-hybrid method using Rag A as the bait to identify proteins binding to Rag A, and we isolated two novel human G proteins, Rag C and Rag D. Rag C demonstrates homology with Rag D (81.1% identity) and with Gtr2p of Saccharomyces cerevisiae (46.1% identity), and it belongs to the Rag A subfamily of the Ras family. Rag C and Rag D contain conserved GTP-binding motifs (PM-1, -2, and -3) in their N-terminal regions. Recombinant glutathione S-transferase fusion protein of Rag C efficiently bound to both [(3)H]GTP and [(3)H]GDP. Rag A was associated with both Rag C and Rag D in their C-terminal regions where a potential leucine zipper motif and a coiled-coil structure were found. Rag C and D were associated with both the GDP and GTP forms of Rag A. Both Rag C and Rag D changed their subcellular localization, depending on the nucleotide-bound state of Rag A. In a similar way, the disruption of S. cerevisiae GTR1 resulted in a change in the localization of Gtr2p.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTR2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Monomeric GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/RRAGA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RRAGB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RRAGC protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7246-57
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11073942-Amino Acid Motifs,
pubmed-meshheading:11073942-Amino Acid Sequence,
pubmed-meshheading:11073942-Binding Sites,
pubmed-meshheading:11073942-Cell Line,
pubmed-meshheading:11073942-Cell Nucleus,
pubmed-meshheading:11073942-Dimerization,
pubmed-meshheading:11073942-Dose-Response Relationship, Drug,
pubmed-meshheading:11073942-Fungal Proteins,
pubmed-meshheading:11073942-GTP-Binding Proteins,
pubmed-meshheading:11073942-Glutathione Transferase,
pubmed-meshheading:11073942-Guanosine Diphosphate,
pubmed-meshheading:11073942-Guanosine Triphosphate,
pubmed-meshheading:11073942-HeLa Cells,
pubmed-meshheading:11073942-Humans,
pubmed-meshheading:11073942-Immunoblotting,
pubmed-meshheading:11073942-Leucine,
pubmed-meshheading:11073942-Microscopy, Fluorescence,
pubmed-meshheading:11073942-Models, Genetic,
pubmed-meshheading:11073942-Molecular Sequence Data,
pubmed-meshheading:11073942-Monomeric GTP-Binding Proteins,
pubmed-meshheading:11073942-Nucleotides,
pubmed-meshheading:11073942-Precipitin Tests,
pubmed-meshheading:11073942-Protein Binding,
pubmed-meshheading:11073942-Protein Structure, Tertiary,
pubmed-meshheading:11073942-Recombinant Fusion Proteins,
pubmed-meshheading:11073942-Recombinant Proteins,
pubmed-meshheading:11073942-Saccharomyces cerevisiae,
pubmed-meshheading:11073942-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11073942-Sequence Homology, Amino Acid,
pubmed-meshheading:11073942-Time Factors,
pubmed-meshheading:11073942-Transfection,
pubmed-meshheading:11073942-Two-Hybrid System Techniques,
pubmed-meshheading:11073942-beta-Galactosidase
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pubmed:year |
2001
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pubmed:articleTitle |
Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B.
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pubmed:affiliation |
Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. sekigu@molbiol.med.kyushu-u.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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