Cloning and characterization of the protein phosphatase 2C of Phytophthora parasitica
Date Issued
2008
Date
2008
Author(s)
Ding, Shan-Yan
Abstract
Phytophthora parasitica Daster (=P. nitcotianae Breda de Haan) is an oomycete plant pathogen. Spreading easily by water, short life cycle, wide host range contributes P. parasitica a worldwide disease. Recent studies show that MAPK pathway is related with the pathogenicity of plant pathogens, such as Colletotrichum spp and Magnaporthe grisea. PP2C negatively regulate MAPK pathway by inactive phospo-MAPKs. We designed specific primers to amplify partial sequence of PP2C from P. parasitica genomes. The entire open reading frame (ORF) was gained by Rapid Amplify cDNA ends (RACE) and named as ppptc1 (Phytophthora parasitica phosphatase two C 1), which encoded 344 amino acids. Ppptc1, which has 40% similarity to human PP2Cα gene, is an one-copy number gene but other homologuesin may exist in the genome of P. parasitica. To express the PPPTC1 protein, the pMAL vector was used to express heterogeneous fusion protein from E. coli. As an alkaline phosphatase, PPPTC1 can dephosphorylate pNPP (para-nitrophenyl phosphate), a non-protein substrate. PPPTC1 also seems to dephosphorylate in vitro with ppmk3, a MAP kinase in P. parasitica. The ppptc1 gene is down-regulated under oxidation, low pH, and high concentration of Ca2+, thus it may involved in MAPK pathway in P. parasitica.
Subjects
alkaline phosphatase
SDGs
File(s)![Thumbnail Image]()
Loading...
Name
ntu-97-R94633016-1.pdf
Size
23.53 KB
Format
Adobe PDF
Checksum
(MD5):1a7139cec081f4dea2a238a78cfb70ba