CRYPTOCHROME STRUCTURE AND SIGNAL TRANSDUCTION Export

@article{citeulike:3874997, abstract = {▪ Abstract  Cryptochromes are photosensory receptors mediating light regulation of growth and development in plants. Since the isolation of the Arabidopsis CRY1 gene in 1993, cryptochromes have been found in every multicellular eukaryote examined. Most plant cryptochromes have a chromophore-binding domain that shares similar structure with DNA photolyase, and a carboxyl terminal extension that contains a DQXVP-acidic-STAES (DAS) domain conserved from moss, to fern, to angiosperm. In Arabidopsis, cryptochromes are nuclear proteins that mediate light control of stem elongation, leaf expansion, photoperiodic flowering, and the circadian clock. Cryptochromes may act by interacting with proteins such as phytochromes, COP1, and clock proteins, or/and chromatin and DNA. Recent studies suggest that cryptochromes undergo a blue light–dependent phosphorylation that affects the conformation, intermolecular interactions, physiological activities, and protein abundance of the photoreceptors.}, author = {Lin, Chentao and Shalitin, Dror}, citeulike-article-id = {3874997}, citeulike-linkout-0 = {http://arjournals.annualreviews.org/doi/abs/10.1146/annurev.arplant.54.110901.160901}, citeulike-linkout-1 = {http://dx.doi.org/10.1146/annurev.arplant.54.110901.160901}, doi = {10.1146/annurev.arplant.54.110901.160901}, journal = {Annual Review of Plant Biology}, keywords = {cryptochromes, review}, number = {1}, pages = {469--496}, posted-at = {2009-10-30 12:48:01}, priority = {2}, title = {CRYPTOCHROME STRUCTURE AND SIGNAL TRANSDUCTION}, url = {http://dx.doi.org/10.1146/annurev.arplant.54.110901.160901}, volume = {54}, year = {2003} }

TY - JOUR ID - citeulike:3874997 L3 - citeulike-article-id:3874997 N2 - ▪ Abstract  Cryptochromes are photosensory receptors mediating light regulation of growth and development in plants. Since the isolation of the Arabidopsis CRY1 gene in 1993, cryptochromes have been found in every multicellular eukaryote examined. Most plant cryptochromes have a chromophore-binding domain that shares similar structure with DNA photolyase, and a carboxyl terminal extension that contains a DQXVP-acidic-STAES (DAS) domain conserved from moss, to fern, to angiosperm. In Arabidopsis, cryptochromes are nuclear proteins that mediate light control of stem elongation, leaf expansion, photoperiodic flowering, and the circadian clock. Cryptochromes may act by interacting with proteins such as phytochromes, COP1, and clock proteins, or/and chromatin and DNA. Recent studies suggest that cryptochromes undergo a blue light–dependent phosphorylation that affects the conformation, intermolecular interactions, physiological activities, and protein abundance of the photoreceptors. IS - 1 JF - Annual Review of Plant Biology EP - 496 TI - CRYPTOCHROME STRUCTURE AND SIGNAL TRANSDUCTION VL - 54 SP - 469 KW - cryptochromes KW - review AU - Lin, Chentao AU - Shalitin, Dror PY - 2003/// UR - http://dx.doi.org/10.1146/annurev.arplant.54.110901.160901 ER -