Abstract
To understand the early signaling steps that regulate cold responses in rice, two-dimensional difference gel electrophoresis (2-D DIGE)(1)was used to study early cold-regulated proteins in rice seedlings. Using mass spectrometry, 32 spots, which represent 26 unique proteins that showed an altered expression level within 5 min of cold treatment were identified. Among these proteins, Western blot analyses confirmed that the cellular phospholipase D α1 (OsPLDα1) protein level was increased as early as 1 min after cold treatment. Genetic studies showed that reducing the expression ofOsPLDα1makes rice plants more sensitive to chilling stress as well as cold acclimation increased freezing tolerance. Correspondingly, cold-regulated proteomic changes and the expression of the cold-responsive C repeat/dehydration-responsive element binding 1 (OsDREB1) family of transcription factors were inhibited in thepldα1mutant. We also found that the expression ofOsPLDα1is directly regulated by OsDREB1A. This transcriptional regulation ofOsPLDα1could provide positive feedback regulation of the cold signal transduction pathway in rice. OsPLDα1 hydrolyzes phosphatidylcholine to produce the signal molecule phosphatidic acid (PA). By lipid-overlay assay, we demonstrated that the rice cold signaling proteins, MAP kinase 6 (OsMPK6) and OsSIZ1, bind directly to PA. Taken together, our results suggest that OsPLDα1 plays a key role in transducing cold signaling in rice by producing PA and regulatingOsDREB1s' expression by OsMPK6, OsSIZ1, and possibly other PA-binding proteins.
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Claims 10
Claim · model-written summary
Cold treatment altered 26 unique proteins represented by 32 spots within five minutes.
- Taxon
- rice
Oryza sativat0
- Treatment
- cold treatmente0
- Outcome
- 26 unique proteinse0
- Value
- 26 unique proteinse0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“32 spots, which represent 26 unique proteins that showed an altered expression level within 5 min of cold treatment were identified”
t0“Rice”
Claim · model-written summary
OsPLDα1 protein level increased within one minute of cold treatment.
- Taxon
- rice
Oryza sativat0
- Treatment
- cold treatmente0
- Gene
- OsPLDα1e0
- Outcome
- protein levele0
- Direction
- increasede0
- Value
- 1 mine0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the cellular phospholipase D α1 (OsPLDα1) protein level was increased as early as 1 min after cold treatment”
t0“Rice”
Claim · model-written summary
Reducing OsPLDα1 expression increased rice sensitivity to chilling.
- Taxon
- rice
Oryza sativae0
- Treatment
- reducing the expression ofOsPLDα1e0
- Gene
- OsPLDα1e0
- Outcome
- sensitive to chilling stresse0
- Direction
- more sensitivee0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“reducing the expression ofOsPLDα1makes rice plants more sensitive to chilling stress”
Claim · model-written summary
Cold acclimation increased freezing tolerance in rice.
- Taxon
- rice
Oryza sativat0
- Treatment
- cold acclimatione0
- Outcome
- freezing tolerancee0
- Direction
- increasede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“cold acclimation increased freezing tolerance”
t0“Rice”
Claim · model-written summary
Cold regulated proteomic changes were inhibited in the pldα1 mutant.
- Taxon
- rice
Oryza sativat0
- Material
- pldα1mutante0
- Treatment
- pldα1mutante0
- Outcome
- cold-regulated proteomic changese0
- Direction
- inhibitede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“cold-regulated proteomic changes and the expression of the cold-responsive C repeat/dehydration-responsive element binding 1 (OsDREB1) family of transcription factors were inhibited in thepldα1mutant”
t0“Rice”
Claim · model-written summary
OsDREB1 family expression was inhibited in the pldα1 mutant.
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the expression of the cold-responsive C repeat/dehydration-responsive element binding 1 (OsDREB1) family of transcription factors were inhibited in thepldα1mutant”
t0“Rice”
Claim · model-written summary
OsDREB1A directly regulates OsPLDα1 expression.
- Taxon
- rice
Oryza sativat0
- Gene
- OsPLDα1e0
- Outcome
- expression ofOsPLDα1e0
- Qualifier
- directly regulated by OsDREB1Ae0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the expression ofOsPLDα1is directly regulated by OsDREB1A”
t0“Rice”
Claim · model-written summary
Rice OsMPK6 binds phosphatidic acid directly.
- Taxon
- rice
Oryza sativae0
- Gene
- OsMPK6e0
- Compound
- PAe0
- Outcome
- bind directly to PAe0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the rice cold signaling proteins, MAP kinase 6 (OsMPK6) and OsSIZ1, bind directly to PA”
Claim · model-written summary
Rice OsSIZ1 binds phosphatidic acid directly.
- Taxon
- rice
Oryza sativae0
- Gene
- OsSIZ1e0
- Compound
- PAe0
- Outcome
- bind directly to PAe0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the rice cold signaling proteins, MAP kinase 6 (OsMPK6) and OsSIZ1, bind directly to PA”
Claim · model-written summary
The authors propose that OsPLDα1 transduces cold signaling through PA production and regulation of OsDREB1 expression.
- Taxon
- rice
Oryza sativae0
- Gene
- OsPLDα1e0
- Compound
- PAe0
- Outcome
- cold signalinge0
- Qualifier
- possibly other PA-binding proteinse0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“OsPLDα1 plays a key role in transducing cold signaling in rice by producing PA and regulatingOsDREB1s' expression by OsMPK6, OsSIZ1, and possibly other PA-binding proteins”
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