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PMID:19417056

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Citation

Wuriyanghan, H, Zhang, B, Cao, WH, Ma, B, Lei, G, Liu, YF, Wei, W, Wu, HJ, Chen, LJ, Chen, HW, Cao, YR, He, SJ, Zhang, WK, Wang, XJ, Chen, SY and Zhang, JS (2009) The ethylene receptor ETR2 delays floral transition and affects starch accumulation in rice. Plant Cell 21:1473-94

Abstract

Ethylene regulates multiple aspects of plant growth and development in dicotyledonous plants; however, its roles in monocotyledonous plants are poorly known. Here, we characterized a subfamily II ethylene receptor, ETHYLENE RESPONSE2 (ETR2), in rice (Oryza sativa). The ETR2 receptor with a diverged His kinase domain is a Ser/Thr kinase, but not a His kinase, and can phosphorylate its receiver domain. Mutation of the N box of the kinase domain abolished the kinase activity of ETR2. Overexpression of ETR2 in transgenic rice plants reduced ethylene sensitivity and delayed floral transition. Conversely, RNA interference (RNAi) plants exhibited early flowering and the ETR2 T-DNA insertion mutant etr2 showed enhanced ethylene sensitivity and early flowering. The effective panicles and seed-setting rate were reduced in the ETR2-overexpressing plants, while thousand-seed weight was substantially enhanced in both the ETR2-RNAi plants and the etr2 mutant compared with controls. Starch granules accumulated in the internodes of the ETR2-overexpressing plants, but not in the etr2 mutant. The GIGANTEA and TERMINAL FLOWER1/CENTRORADIALIS homolog (RCN1) that cause delayed flowering were upregulated in ETR2-overexpressing plants but downregulated in the etr2 mutant. Conversely, the alpha-amylase gene RAmy3D was suppressed in ETR2-overexpressing plants but enhanced in the etr2 mutant. Thus, ETR2 may delay flowering and cause starch accumulation in stems by regulating downstream genes.

Links

PubMed PMC2700534 Online version:10.1105/tpc.108.065391

Keywords

Amino Acid Sequence; Binding Sites; Ethylenes/metabolism; Flowers/genetics; Flowers/growth & development; Flowers/metabolism; Molecular Sequence Data; Mutagenesis, Site-Directed; Oryza sativa/genetics; Oryza sativa/growth & development; Oryza sativa/metabolism; Phosphorylation; Plant Proteins/chemistry; Plant Proteins/genetics; Plant Proteins/physiology; Plants, Genetically Modified/growth & development; Plants, Genetically Modified/metabolism; Protein Structure, Tertiary; RNA Interference; Receptors, Cell Surface/chemistry; Receptors, Cell Surface/genetics; Receptors, Cell Surface/physiology; Sequence Alignment; Starch/metabolism; alpha-Amylases/genetics; alpha-Amylases/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ORYSJ:ETR2

GO:0009723: response to ethylene stimulus

ECO:0000315:

P

Figure 3 C and D show altered response to ethylene in ETR2 overexpressors.

complete
CACAO 5549

ORYSJ:ETR2

GO:2000904: regulation of starch metabolic process

ECO:0000315:

P

Figure 6A shows ETR2 overexpresssors have increased starch storage in its internodes, and etr2 mutants have reduced starch storage in the first internode.

complete
CACAO 5550

ORYSJ:ETR2

GO:0006355: regulation of transcription, DNA-dependent

ECO:0000315:

P

Figure 7 shows ETR2 over and under expressing mutants have altered levels of gene transcription.

complete
CACAO 5551

ORYSJ:ETR2

GO:0004674: protein serine/threonine kinase activity

ECO:0000314:

F

Figure 2F

complete
CACAO 5548

ORYSJ:ETR2

enables

GO:0004674: protein serine/threonine kinase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

ORYSJ:ETR2

involved_in

GO:0009723: response to ethylene

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

ORYSJ:ETR2

involved_in

GO:2000904: regulation of starch metabolic process

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

ORYSJ:ETR2

involved_in

GO:0006355: regulation of transcription, DNA-templated

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete


See also

References

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