Publications (2)3.34 Total impact
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Article: Molecular cloning and expression analysis of the cell-wall invertase gene family in rice (Oryza sativa L.).
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ABSTRACT: Cell-wall invertase (CIN) catalyzes the hydrolysis of sucrose into glucose and fructose for the supply of carbohydrates to sink organs via an apoplastic pathway. To study the CIN genes in rice (Oryza sativa L.), we isolated cDNA clones showing amino acid similarity to the plant cell wall invertase proteins from a search of rice sequence databases. Profile analyses revealed that the cloned genes are expressed in unique patterns in various organs. For example, transcripts of OsCIN1, OsCIN2, OsCIN4, and OsCIN7 were detected in immature seeds whereas OsCIN3 gene expression was flower-specific. Further transcript analysis of these genes expressed in developing seeds indicated that OsCIN1, OsCIN2, and OsCIN7 might play an important role involving sucrose partitioning to the embryo and endosperm. Sucrose, a substrate of CINs, induced the accumulation of OsCIN1 transcripts in excised leaves and OsCIN2 in immature seeds, while the level of OsCIN5 was significantly down-regulated in excised leaves treated with sucrose. Infecting the tissues with rice blast (Magnaporthe grisea) as a biotic stressor increased the expression of OsCIN1, OsCIN4, and OsCIN5, suggesting that these genes may participate in a switch in metabolism to resist pathogen invasion. These results demonstrate that OsCIN genes play diverse roles involving the regulation of metabolism, growth, development, and stress responses.Plant Cell Reports 07/2005; 24(4):225-36. · 2.27 Impact Factor -
Article: Potential target gene and protein interaction ofPimpinella brachycarpa HD-Zip protein, Phz4 by yeast two-hybrid system
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ABSTRACT: The yeast two-hybrid system was used to investigate dimerization between proteins ofPhz2 andPhz4 clones of the homeodomain-leucine zipper family which were obtained by screening aPimpinella brachycarpa shoot-tip cDNA library. Assays showed that Phz4 formed a homo rather than a heterodimer with Phz2. In addition, we isolated cDNA clones,Phyb1, Phyb2, andPhyb3, that encode proteins interacting with Phz4. Although Phyb1 is not a HD-Zip protein, the activity of interaction between Phyb1 and Phz4 was, surprisingly, stronger than that of the homodimerization of Phz4. The analysis of interacting parts indicated that from 1 bp to 466 bp of Phyb1, there was no interaction with Phz4, but from 467 bp to 593 bp, interactions were found with the N-terminal and C-terminal regions, except for HD-Zip of Phz4. This region ofPhyb1 contained a nuclear localization signal. DNA-binding analysis showed that the Phz4 HD-Zip domain recognized the [T(C/G)ATTG] core sequence and the region containing the [TCATTG] motif, which is, in itself, a promoter in vitro.Journal of Plant Biology 04/1999; 42(4):302-309. · 1.07 Impact Factor
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Institutions
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1999
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Seoul National University
- Department of Biological Sciences
Seoul, Seoul, South Korea
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