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Cho, Moo Je
Ulsan National Institute of Science and Technology
Research Interests
  • Calcium Signaling

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Characterization of two fungal-elicitor-induced rice cDNAs encoding functional homologues of the rab-specific GDP-dissociation inhibitor

Cited 23 times inthomson ciCited 21 times inthomson ci
Title
Characterization of two fungal-elicitor-induced rice cDNAs encoding functional homologues of the rab-specific GDP-dissociation inhibitor
Author
Kim, WYKim, CYCheong, NEChoi, YOLee, KOLee, SHPark, JBNakano, ABahk, JDCho, Moo JeLee, SY
Keywords
Differential display;  Functional analysis;  Fungal elicitor treatment;  Oryza (rab-GDIs);  Pathogen signaling;  Rab-specific GDP dissociation inhibitor
Issue Date
199911
Publisher
SPRINGER
Citation
PLANTA, v.210, no.1, pp.143 - 149
Abstract
By using the mRNA differential display approach to isolate defense signaling genes active at the early stage of fungal infection two cDNA fragments with high sequence homology to rab-specific GDP-dissociation inhibitors (GDIs) were identified in rice (Oryza sativa L.) suspension cells. Using polymerase-chain-reaction products as probes, two full-length cDNA clones were isolated from a cDNA library of fungal-elicitor-treated rice, and designated as OsGDI1 and OsGDI2. The deduced amino acid sequences of the isolated cDNAs exhibited substantial homology to Arabidopsis rab-GDIs. Northern analysis revealed that transcripts detected with the 3'-gene-specific DNA probes accumulated to high levels within 30 min after treatment with a fungal elicitor derived from Magnaporthe grisea. The functionality of the OsGDIs was demonstrated by their ability to rescue the Sec19 mutant of Saccharomyces cerevisiae which is defective in vesicle transport. The proteins, expressed in Escherichia coli, cross-reacted with a polyclonal antibody prepared against bovine rab-GDI. Like bovine rab-GDI, the OsGDI proteins efficiently dissociated rab3A from bovine synaptic membranes. Using the two-hybrid system, it was shown that the OsGDIs specifically interact with the small GTP-binding proteins belonging to the rab subfamily. The specific interaction was also demonstrated in vitro by glutathione S-transferase resin pull-down assay.
URI
http://scholarworks.unist.ac.kr/handle/201301/6360
DOI
http://dx.doi.org/10.1007/s004250050663
ISSN
0032-0935
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