TY - JOUR
T1 - Identification of a new cryptochrome class
T2 - Structure, function, and evolution
AU - Brudler, Ronald
AU - Hitomi, Kenichi
AU - Daiyasu, Hiromi
AU - Toh, Hiroyuki
AU - Kucho, Ken Ichi
AU - Ishiura, Masahiro
AU - Kanehisa, Minoru
AU - Roberts, Victoria A.
AU - Todo, Takeshi
AU - Tainer, John A.
AU - Getzoff, Elizabeth D.
N1 - Funding Information:
We thank A. Arvai for assistance with AMoRe and CNS, Drs. T. Oyama and T. Imaizumi for providing Arabidopsis RNA and cDNA library, Dr. K. Okamoto for construction of the knockout mutant, and Mrs. E. Sato for assistance with protein preparation. K.H. thanks Dr. Ishiura for continuous encouragement. Diffraction data were collected at the Stanford Synchrotron Radiation Laboratory (SSRL), which is operated by the Department of Energy, Office of Basic Energy Sciences. This work was supported by grant GM37684 from the NIH to E.D.G. and a Skaggs fellowship to K.H.
PY - 2003/1/1
Y1 - 2003/1/1
N2 - Cryptochrome flavoproteins, which share sequence homology with light-dependent DNA repair photolyases, function as photoreceptors in plants and circadian clock components in animals. Here, we coupled sequencing of an Arabidopsis cryptochrome gene with phylogenetic, structural, and functional analyses to identify a new cryptochrome class (cryptochrome DASH) in bacteria and plants, suggesting that cryptochromes evolved before the divergence of eukaryotes and prokaryotes. The cryptochrome crystallographic structure, reported here for Synechocystis cryptochrome DASH, reveals commonalities with photolyases in DNA binding and redox-dependent function, despite distinct active-site and interaction surface features. Whole genome transcriptional profiling together with experimental confirmation of DNA binding indicated that Synechocystis cryptochrome DASH functions as a transcriptional repressor.
AB - Cryptochrome flavoproteins, which share sequence homology with light-dependent DNA repair photolyases, function as photoreceptors in plants and circadian clock components in animals. Here, we coupled sequencing of an Arabidopsis cryptochrome gene with phylogenetic, structural, and functional analyses to identify a new cryptochrome class (cryptochrome DASH) in bacteria and plants, suggesting that cryptochromes evolved before the divergence of eukaryotes and prokaryotes. The cryptochrome crystallographic structure, reported here for Synechocystis cryptochrome DASH, reveals commonalities with photolyases in DNA binding and redox-dependent function, despite distinct active-site and interaction surface features. Whole genome transcriptional profiling together with experimental confirmation of DNA binding indicated that Synechocystis cryptochrome DASH functions as a transcriptional repressor.
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U2 - 10.1016/S1097-2765(03)00008-X
DO - 10.1016/S1097-2765(03)00008-X
M3 - Article
C2 - 12535521
AN - SCOPUS:0037249267
SN - 1097-2765
VL - 11
SP - 59
EP - 67
JO - Molecular cell
JF - Molecular cell
IS - 1
ER -