Abstract
Two cryptochrome proteins, CRY1 and CRY2, occur in plants and animals. CRY1 regulates the circadian clock in a light-dependent fashion in insects and plants. Also in plants, blue light photoreception can be used to cue developmental signals. Despite much research on the topic, the specific way that the pterin and flavin chromophores function in these proteins in Arabidopsis thaliana is still poorly understood. The goal of this research was to clone and express the Arabidopsis CRY1 protein in an E. coli expression system. The Arabidopsis CRY1 coding sequence was commercially synthesized and cloned into a pDEST vector and expressed with N-terminal GST and His tags. The expressed fusion proteins were purified using Glutathione agarose or Ni-NTA affinity chromatography. Purified proteins will be used for structural and functional analysis.
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