Article
RAR1 and HSP90 form a complex with Rac/Rop GTPase and function in innate-immune responses in rice.
Laboratory of Plant Molecular Genetics, Nara Institute of Science and Technology, Ikoma 630-0101, Japan.
The Plant Cell (impact factor:
8.99).
01/2008;
19(12):4035-45.
DOI:10.1105/tpc.107.055517
pp.4035-45
Source: PubMed
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Article: Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation.
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ABSTRACT: The molecular mechanisms by which oncogenic tyrosine kinases induce cellular transformation are unclear. Herbimycin A, geldanamycin, and certain other benzoquinone ansamycins display an unusual capacity to revert tyrosine kinase-induced oncogenic transformation. As an approach to the study of v-src-mediated transformation, we examined ansamycin action in transformed cells and found that drug-induced reversion could be achieved without direct inhibition of src phosphorylating activity. To identify mechanisms other than kinase inhibition for drug-mediated reversion, we prepared a solid phase-immobilized geldanamycin derivative and affinity precipitated the molecular targets with which the drug interacted. In a range of cell lines, immobilized geldanamycin bound elements of a major class of heat shock protein (HSP90) in a stable and pharmacologically specific manner. Consistent with these binding data, we found that soluble geldanamycin and herbimycin A inhibited specifically the formation of a previously described src-HSP90 heteroprotein complex. A related benzoquinone ansamycin that failed to revert transformed cells did not inhibit the formation of this complex. These results demonstrate that HSP participation in multimolecular complex formation is required for src-mediated transformation and can provide a target for drug modulation.Proceedings of the National Academy of Sciences 09/1994; 91(18):8324-8. · 9.68 Impact Factor -
Article: Ubiquitin ligase-associated protein SGT1 is required for host and nonhost disease resistance in plants.
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ABSTRACT: Homologues of the yeast ubiquitin ligase-associated protein SGT1 are required for disease resistance in plants mediated by nucleotide-binding site/leucine-rich repeat (NBS-LRR) proteins. Here, by silencing SGT1 in Nicotiana benthamiana, we extend these findings and demonstrate that SGT1 has an unexpectedly general role in disease resistance. It is required for resistance responses mediated by NBS-LRR and other R proteins in which pathogen-derived elicitors are recognized either inside or outside the host plant cell. A requirement also exists for SGT1 in nonhost resistance in which all known members of a host species are resistant against every characterized isolate of a pathogen. Our findings show that silencing SGT1 affects diverse types of disease resistance in plants and support the idea that R protein-mediated and nonhost resistance may involve similar mechanisms.Proceedings of the National Academy of Sciences 09/2002; 99(16):10865-9. · 9.68 Impact Factor
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Keywords
blast fungus Magnaporthe grisea
compatible race
functional relationships
heat shock protein 90 kD
mammalian innate immunity
Mla12 resistance
molecular function
molecular level
Os Rac1
Os RAR1-RNA interference
Os RAR1-RNAi
plant species
protein complexes
protein levels
Rac1 complex
Rac1 forms
Rac1-mediated enhancement
rice cell culture
rice cell cultures
rice cells