Human blue-light photoreceptor hCRY2

Details Human blue-light photoreceptor hCRY2 Human blue-light photoreceptor hCRY2

1998-06-26

2003-05-27

Prouty, Rebecca E. (Department: 1652)

Chemistry: natural resins or derivatives; peptides or proteins;

Proteins, i.e., more than 100 amino acid residues

C435S183000, C435S069100, C435S320100, C435S325000, C435S252300, C435S006120, C536S023100

Reexamination Certificate

active

06569994

ABSTRACT:

BACKGROUND OF THE INVENTION
1. Field of the Invention
The present invention relates to a novel human blue-light photoreceptor. More specifically, isolated nucleic acid molecules are provided encoding a human blue-light photoreceptor. Human blue-light photoreceptor polypeptides are also provided, as are vectors, host cells, antibodies, and recombinant methods for producing the same.
2. Related Art
In many organisms, the photolyase/photoreceptor family of proteins mediates DNA repair. In plants, certain developmental processes are regulated by blue-light. This regulation occurs by a photoinduced electron transfer reaction (Taylor, J. S.,
Acc. Chem. Res
. 27:76-82 (1994); Menkens, A. E. et al.,
Biochemistry
34:6892-6899 (1995); Heelis, P. F. et al.,
Photochem. Photobiol
. 95:89-98 (1996); and Sancar A.,
Science
272:48-49 (1996)). Indeed, to date, most of the work concerning blue-light photoreceptors has been conducted in plants (Cashmore, A. R. et al.,
International Patent Application
WO 96/01897 (1996); Hinnemann, H.,
Photochem. Photobol
. 61:22-31(1995); Short, T. W. et al.,
Annu. Rev. Plant. Physiol. Plant Mol. Biol
. 45:143-171 (1994); Hohl, N. et al.,
Photochem. Photobiol
. 55:239-245 (1992)) and fungi (Dunlap, J. C.,
Annu. Rev. Physiol
. 55:683-728 (1993)). In plants, blue-light induces responses such as photomorphogenesis, phototropism and hypocotyl elongation. In particular, it has been demonstrated that the HY4 gene of
A. thaliana
, which encodes the CRY1 protein, is required for blue-light induced hypocotyl elongation (Ahmad, M., et al.,
Nature
366:162-166 (1993)).
In animals, most of the work on light response (other than vision) has been concentrated on circadian clocks. In
D. melanogaster
, two genes have been cloned, timeless and period, which regulate the circadian rhythm (Myers, M. P. et al.,
Science
270:805-808 (1995); Gekakis, N. et al.,
Science
270:811-814 (1995)). Both appear to be transcription factors for which activity is regulated by light. A mutation in the golden hamster tau gene disrupts the circadian clock Ralph and Menaker, 1988). Three mouse genes, CLOCK, ICER, and CREM, which are involved in the control of circadian rhythm, have been investigated in some detail (Vitaterna et al., M. H. et al.,
Science
264:719-725 (1994); Sassone-Corsi P. A,
Rev. Cell Dev. Biol
. 11:355-377 (1995); Foulkes, N. S. et al.,
Nature
381:83-85 (1996)). Each of these three gene products appears to be a transcriptional repressor for which activity is regulated by light. However, how the light signal is transmitted to these transcriptional regulators is not known.
Currently, the photolyase/photoreceptor protein family is known to contain three members: the cyclobutane pyrimidine dimer (Pyr< >Pyr) photolyase (photolyase), the (6-4) photolyase, and the blue-light photoreceptor (Todo, T. et al.,
Science
272:109-112 (1996)). The gene for the classical Pyr< >Pyr photolyase has been cloned and the enzyme has been purified from many organisms, including
Escherichia coli, Saccharomyces cerevisiae, Drosophila melanogaster
, and
Carassius auratus
(Sancar, A,
Mutation Res
. 236:147-160(1990); Kato, T. et al.,
Nucl. Acids Res
. 22:41194124 (1994); and Yasui, A et al.,
EMBO J
. 13:6143-6151 (1994). The (6-4) photolyase has been found in
D. melanogaster
(Todo, T. et al.,
Nature
361:371-374 (1993); Kim, S. T. et al.,
J. Biol. Chem.
269:8535-8540 (1994)),
Xenopus laevis
, and
Crotalus atrox
(Kim, S. T. et al.,
Photochem. Photobiol
. 63:292-295 (1996)).
Concerning the cloning of (6-4) photolyase genes, only the Drosophila gene has been cloned and sequenced (Todo, T. et al.,
Science
272:109-112 (1996)). The genes for the apoproteins of the blue-light photoreceptors of
Arabidopsis thaliana
(Ahmad, M.,
Nature
366:162-166 (1993)),
Sinapis alba
(Batschauer, A,
Plant J
. 4:705-709 (1993); Malhotra, K. et al.,
Biochemistry
34:6892-6899 (1995)), and
Chlamydomonas reinhardtii
(Small, G. D., et al.,
Plant Molec. Biol
. 28:433-454 (1995)) have been cloned and sequenced. The photoreceptors of
A. thaliana
(Malhotra, K. et al.,
Biochemistry
34:6892-6899 (1995); Lin, C. et al.,
Science
269: 968-970 (1995)) and
S. alba
(Malhotra, K. et al.,
Biochemistry
34:6892-6899 (1995)) have been purified and characterized.
Circadian regulation of human and animal physiology, and particularly circadian regulation mediated by blue-light photoreceptors, is poorly understood. Thus, there is a need for an isolated human blue-light photoreceptor gene, the polypeptide encoded by that gene, and antibodies specific for that polypeptide.
SUMMARY OF THE INVENTION
The present invention provides isolated nucleic acid molecules comprising a polynucleotide encoding the human blue-light photoreceptor hCRY2 [hereinafter “hCRY2”] receptor having the amino acid sequence shown in SEQ ID NO:2 or the amino acid sequence encoded by the cDNA clone deposited in a bacterial host as ATCC Deposit Number 97769 on Oct. 22, 1996.
The present invention also relates to recombinant vectors, which include the isolated nucleic acid molecules of the present invention, to host cells containing the recombinant vectors, to host cells containing an isolated polypeptide, as well as to methods of making such vectors and host cells and for using them for production of hCRY2 polypeptides or peptides by recombinant techniques.
The invention further provides an isolated hCRY2 polypeptide having an amino acid sequence encoded by a polynucleotide described herein.
The invention further provides isolated antibodies that bind specifically to the full length hCRY2 receptor, the mature hCRY2 receptor, the hCRY2 receptor extracellular domain, the hCRY2 receptor transmembrane domain, the hCRY2 receptor intracellular domain, and epitope-bearing portions of the hCRY2 receptor.


REFERENCES:
patent: WO 96/01897 (1996-01-01), None
Griffin et al., Science 286:768-771, 1999.*
Van der Horst et al., Nature 398:627-630, 1999.*
Kume et al., Cell 98:193-205, 1999.*
Bork, Genome Research, 10:348-400, 2000.*
Broun et al., Science 282:1315-1317, 1998.*
Van de Loo et al., Proc. Natl. Acad. Sci. 92:6743-6747, 1995.*
Hillier, L. et al., GenBank Database, Accession No. H21100, Jul. 1995.*
Kloesgen, R. et al., GenBank Database, Accession No. P04713, Aug. 1987.*
Todo, T. et al., Science, vol. 272, pp. 109-112, Apr. 5, 1996.*
Adams, M.D. et al., “Complementary DNA Sequencing: Expressed Sequence Tags and Human Genome Project,”Science252:1651-1656 (1991).
Adams, M.D. et al., “Sequence identification of 2,375 human brain genes,”Nature355:632-634 (1992).
Adams, M.D. et al., “Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence,”Nature377:3-17 (Sep. 1995).
Ahmad, M. and A.R. Cashmore, “HY4 gene ofA. thalianaencodes a protein with characteristics of a blue-light photoreceptor,”Nature366:162-166 (1993).
Ahmad, M. and A.R. Cashmore, “Seeing blue: the discovery of cryptochrome,”Plant Mol. Biol.30:851-861 (Mar. 1996).
Batschauer, A., “A plant gene for photolyase: an enzyme catalyzing the repair of UV-light-induced DNA damage,”Plant J.4(4):705-709 (1993).
Dunlap, J.C., “Genetic Analysis of Circadian Clocks,”Annu. Rev. Physiol.55:683-728 (1993).
Hohl, N. et al., “Altered Pterin Patterns in Photobehavioral Mutants ofPhycomyces blakesleeanus,” Photochem.&Photobiol.55(2):239-245 (1992).
Kato, T., Jr. et al., “Cloning of a marsupial DNA photolyase gene and the lack of related nucleotide sequences in placental mammals,”Nucl. Acids Res.22(20):4119-4124 (1994).
Kim, S.-T. et al., “Characterization of (6-4) Photoproduct DNA Photolyase,”J. Biol. Chem.269(11):8535-8540 (1994).
Kim, S.-T. et al., “Purification and Partial Characterization of (6-4) Photoproduct DNA Photolyase fromXenopus laevis,” Photochem.&Photobiol.63(3):292-295 (Mar. 1996).
Kim, S.-T., et al. “Purification and characterization ofDrosophila melanogasterphotolyase,”Mut. Res.363:97-104 (Jun. 1996).
Ley, R.D., “Photoreactivation in humans,”Proc. Natl. Acad. Sci. USA90:4337 (1993).
Li, Y.F. et al., “E

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