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Identification of a new cryptochrome class: Structure, function, and evolution

Academic Article
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Overview

authors

  • Brudler, R.
  • Hitomi, K.
  • Daiyasu, H.
  • Toh, H.
  • Kucho, K.
  • Ishiura, M.
  • Kanehisa, M.
  • Roberts, V. A.
  • Todo, T.
  • Tainer, John
  • Getzoff, Elizabeth

publication date

  • January 2003

journal

  • Molecular Cell  Journal

abstract

  • 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.

subject areas

  • Amino Acid Sequence
  • Animals
  • Arabidopsis
  • Arabidopsis Proteins
  • Bacterial Proteins
  • Binding Sites
  • Biological Clocks
  • Cryptochromes
  • Crystallography, X-Ray
  • Cyanobacteria
  • Deoxyribodipyrimidine Photo-Lyase
  • Drosophila Proteins
  • Evolution, Molecular
  • Eye Proteins
  • Flavoproteins
  • Genes, Plant
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Oligonucleotide Array Sequence Analysis
  • Photoreceptor Cells, Invertebrate
  • Phylogeny
  • Receptors, G-Protein-Coupled
  • Sequence Alignment
  • Sequence Analysis, DNA
  • Substrate Specificity
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Identity

International Standard Serial Number (ISSN)

  • 1097-2765

Digital Object Identifier (DOI)

  • 10.1016/s1097-2765(03)00008-x

PubMed ID

  • 12535521
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Additional Document Info

start page

  • 59

end page

  • 67

volume

  • 11

issue

  • 1

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