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Article: OsPFA-DSP1, a rice protein tyrosine phosphatase, negatively regulates drought stress responses in transgenic tobacco and rice plants

TitleOsPFA-DSP1, a rice protein tyrosine phosphatase, negatively regulates drought stress responses in transgenic tobacco and rice plants
Authors
KeywordsDrought stress
OsPFA-DSP1
PFA-DSPs
Protein tyrosine phosphatase
Issue Date2012
Citation
Plant Cell Reports, 2012, v. 31, n. 6, p. 1021-1032 How to Cite?
AbstractDephosphorylation 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 OsPFA-DSP1 mRNA was induced by drought stress. Transfection of rice protoplasts showed that OsPFA-DSP1 accumulated in both the cytoplasm and nucleus. Ectopic overexpression of OsPFA-DSP1 in tobacco increased sensitivity to drought stress and insensitivity to ABA-induced stomatal closure and inhibition of stomatal opening. Furthermore, overexpression of OsPFA-DSP1 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. © 2012 Springer-Verlag.
Persistent Identifierhttp://hdl.handle.net/10722/316434
ISSN
2023 Impact Factor: 5.3
2023 SCImago Journal Rankings: 1.319
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLiu, Bing-
dc.contributor.authorFan, Jieqiong-
dc.contributor.authorZhang, Yang-
dc.contributor.authorMu, Peiqiang-
dc.contributor.authorWang, Peng-
dc.contributor.authorSu, Jianbin-
dc.contributor.authorLai, Huihuang-
dc.contributor.authorLi, Shaowu-
dc.contributor.authorFeng, Dongru-
dc.contributor.authorWang, Jinfa-
dc.contributor.authorWang, Hongbin-
dc.date.accessioned2022-09-14T11:40:26Z-
dc.date.available2022-09-14T11:40:26Z-
dc.date.issued2012-
dc.identifier.citationPlant Cell Reports, 2012, v. 31, n. 6, p. 1021-1032-
dc.identifier.issn0721-7714-
dc.identifier.urihttp://hdl.handle.net/10722/316434-
dc.description.abstractDephosphorylation 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 OsPFA-DSP1 mRNA was induced by drought stress. Transfection of rice protoplasts showed that OsPFA-DSP1 accumulated in both the cytoplasm and nucleus. Ectopic overexpression of OsPFA-DSP1 in tobacco increased sensitivity to drought stress and insensitivity to ABA-induced stomatal closure and inhibition of stomatal opening. Furthermore, overexpression of OsPFA-DSP1 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. © 2012 Springer-Verlag.-
dc.languageeng-
dc.relation.ispartofPlant Cell Reports-
dc.subjectDrought stress-
dc.subjectOsPFA-DSP1-
dc.subjectPFA-DSPs-
dc.subjectProtein tyrosine phosphatase-
dc.titleOsPFA-DSP1, a rice protein tyrosine phosphatase, negatively regulates drought stress responses in transgenic tobacco and rice plants-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1007/s00299-011-1220-x-
dc.identifier.pmid22218675-
dc.identifier.scopuseid_2-s2.0-84861199013-
dc.identifier.volume31-
dc.identifier.issue6-
dc.identifier.spage1021-
dc.identifier.epage1032-
dc.identifier.isiWOS:000304145700006-

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