The cryptochrome blue light photoreceptors were first described in the plant Arabidopsis. These photoreceptors are widespread, if not ubiquitous, throughout the plant kingdom, apparently present in all higher plants as well as ferns and algae. Cryptochrome-mediated blue light signaling affects a variety of plant processes including stem elongation, pigment production, gene expression, flowering time, and the entrainment of circadian rhythms. Cryptochromes have also been described for animals, including humans, where they play an essential role in circadian behavioral rhythms. Dark-grown transgenic Arabidopsis plants expressing the C-terminal domain of cryptochrome exhibit features that are normally associated with light-grown plants, indicating that the signaling properties of cryptochrome reside within this C-terminal domain. Apparently this signaling potential is repressed in the native cryptochrome molecule in the dark, this repression being overridden by the action of light. Here we propose to define the factors that are necessary to reconstruct in vitro the light-dependent signaling activity of cryptochrome. In addition, we will define the mechanism and the domain of the cryptochrome protein necessary for repressing cryptochrome signaling activity in the dark. We will use microarrays to identify genes whose expression is dependent on cryptochrome and we will perform chromatin immunoprecipitation studies to characterize the association of cryptochrome and other signaling partners with chromatin. Finally, we will further characterize new mutants of Arabidopsis that, like cryptochrome mutants, are selectively deficient in blue light signaling and therefore define new genes that regulate the light signaling process.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM051956-09
Application #
6582684
Study Section
Cell Development and Function Integrated Review Group (CDF)
Program Officer
Anderson, James J
Project Start
1994-12-01
Project End
2007-06-30
Budget Start
2003-07-01
Budget End
2004-06-30
Support Year
9
Fiscal Year
2003
Total Cost
$364,550
Indirect Cost
Name
University of Pennsylvania
Department
Biology
Type
Schools of Arts and Sciences
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104
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Cashmore, A R; Jarillo, J A; Wu, Y J et al. (1999) Cryptochromes: blue light receptors for plants and animals. Science 284:760-5
Cashmore, A R (1998) Higher-plant phytochrome: ""I used to date histidine, but now I prefer serine"". Proc Natl Acad Sci U S A 95:13358-60
Ahmad, M; Jarillo, J A; Cashmore, A R (1998) Chimeric proteins between cry1 and cry2 Arabidopsis blue light photoreceptors indicate overlapping functions and varying protein stability. Plant Cell 10:197-207
Lin, C; Yang, H; Guo, H et al. (1998) Enhancement of blue-light sensitivity of Arabidopsis seedlings by a blue light receptor cryptochrome 2. Proc Natl Acad Sci U S A 95:2686-90
Ahmad, M; Jarillo, J A; Klimczak, L J et al. (1997) An enzyme similar to animal type II photolyases mediates photoreactivation in Arabidopsis. Plant Cell 9:199-207
Ahmad, M; Cashmore, A R (1997) The blue-light receptor cryptochrome 1 shows functional dependence on phytochrome A or phytochrome B in Arabidopsis thaliana. Plant J 11:421-7
Lin, C; Ahmad, M; Cashmore, A R (1996) Arabidopsis cryptochrome 1 is a soluble protein mediating blue light-dependent regulation of plant growth and development. Plant J 10:893-902

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