Glyceraldehyde-3-phosphate dehydro- genase (GAPDH) is a multifunctional protein well defined in eukaryotes, especially in mammalian and Saccharomyces cerevisiae. Using the method of suppression subtractive hybridizati...Glyceraldehyde-3-phosphate dehydro- genase (GAPDH) is a multifunctional protein well defined in eukaryotes, especially in mammalian and Saccharomyces cerevisiae. Using the method of suppression subtractive hybridization (SSH), we identified a Phytophthora sojae cDNA coding GAPDH, which was up-regulated during the early stage of soybean infection. The termed PsGapdh gene pos- sessed three copies in the P. sojae genome. Its amino acid sequence harbored overall conserved domain of GADPH, homologous closest to GapC1 of Achlya bisexualis (oomycete) and adjoined to GapC2s of Odontella sinensis and Phaeodactylum tricornutum (diatom), on the C-Ⅱ branch of subfamily GapC in phylogeny tree of GAPDH. The transcrip- tional level of PsGapdh was up-regulated throughout early infection. Heterogenous expression of PsGapdh in the yeast tdh1-deleted mutant could rescue growth arrest under continuous exposure to H2O2. These results indicated active roles of PsGapdh in patho- gen-host interaction and anti-oxidation.展开更多
文摘Glyceraldehyde-3-phosphate dehydro- genase (GAPDH) is a multifunctional protein well defined in eukaryotes, especially in mammalian and Saccharomyces cerevisiae. Using the method of suppression subtractive hybridization (SSH), we identified a Phytophthora sojae cDNA coding GAPDH, which was up-regulated during the early stage of soybean infection. The termed PsGapdh gene pos- sessed three copies in the P. sojae genome. Its amino acid sequence harbored overall conserved domain of GADPH, homologous closest to GapC1 of Achlya bisexualis (oomycete) and adjoined to GapC2s of Odontella sinensis and Phaeodactylum tricornutum (diatom), on the C-Ⅱ branch of subfamily GapC in phylogeny tree of GAPDH. The transcrip- tional level of PsGapdh was up-regulated throughout early infection. Heterogenous expression of PsGapdh in the yeast tdh1-deleted mutant could rescue growth arrest under continuous exposure to H2O2. These results indicated active roles of PsGapdh in patho- gen-host interaction and anti-oxidation.
