Phytochrome-interacting protein and a use thereof

Details Phytochrome-interacting protein and a use thereof Phytochrome-interacting protein and a use thereof

2005-02-28

2010-06-01

Baum, Stuart F. (Department: 1638)

Multicellular living organisms and unmodified parts thereof and

Plant, seedling, plant seed, or plant part, per se

Higher plant, seedling, plant seed, or plant part

C800S278000, C800S290000, C800S320000

Reexamination Certificate

active

07728193

ABSTRACT:
The present invention relates to a novel protein interacting with phytochromes and use thereof, and more particularly, to a polypeptide having either an amino acid sequence set forth in SEQ ID NO: 4 or an amino acid sequence having at least 70% with said amino acid sequence, and use thereof. The polypeptide interacts with phytochromes A and B, and the TPR domain present at the N-terminal region of the polypeptide is involved in the interaction. Also, a PP2A catalytic domain (PP2Ac) having phosphatase activity is present at the C-terminal region of the polypeptide. The polypeptide can be used as a phosphatase, and is useful in the production of plants sensitive to light signal transduction. Furthermore, the TPR domain present in the polypeptide is useful in the production of dwarf plants.

REFERENCES:
patent: 6660511 (2003-12-01), Luo et al.
NCBI Accession No. AAQ22649 dated Aug. 12, 2003.
Fankhauser et al., “Light receptor kinases in plants,”Current Biology, 1999, vol. 9, pp. R123-R126, Elsevier Science, Oxford, England.
Neff et al., “Light: an indicator of time and place,”Genes&Development, 2000, vol. 14, pp. 257-271, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
Das et al., “The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions,”The EMBO Journal, 1998, vol. 17, No. 5, pp. 1192-1199, Oxford University Press, Oxford, England.

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