Journal
PLANT CELL REPORTS
Volume 31, Issue 6, Pages 1021-1032Publisher
SPRINGER
DOI: 10.1007/s00299-011-1220-x
Keywords
Protein tyrosine phosphatase; PFA-DSPs; Drought stress; OsPFA-DSP1
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Funding
- National Natural Science Foundation of China [30800600, 30970237]
- Natural Science Foundation of Guangdong Province, P. R. China [8151027501000016]
- Fundamental Research Funds for the Central Universities [10lgpy34]
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Dephosphorylation plays a pivotal role in regulating plant growth, development and abiotic/biotic stress responses. Here, we characterized a plant and fungi atypical dual-specificity phosphatase (PFA-DSP) subfamily member, OsPFA-DSP1, from rice. OsPFA-DSP1 was determined to be a functional protein tyrosine phosphatase (PTP) in vitro using phosphatase activity assays. Quantitative real-time PCR and GENEVESTIGATOR analysis showed that - mRNA was induced by drought stress. Transfection of rice protoplasts showed that OsPFA-DSP1 accumulated in both the cytoplasm and nucleus. Ectopic overexpression of - in tobacco increased sensitivity to drought stress and insensitivity to ABA-induced stomatal closure and inhibition of stomatal opening. Furthermore, overexpression of - in rice also increased sensitivity to drought stress. These results indicated that OsPFA-DSP1 is a functional PTP and may act as a negative regulator in drought stress responses.
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