Disease relevance of phr6-4

• The recombinant protein did not show photolyase activity for either cyclobutane pyrimidine dimers or 6-4 photoproducts in vitro as well as in vivo in Escherichia coli host cells, suggesting that the protein is not a DNA repair enzyme but a blue-light photoreceptor [1].

High impact information on phr6-4

• They absorb light and transmit the electromagnetic signal to the molecular clock using a pterin and flavin adenine dinucleotide (FAD) as chromophore/cofactors, and are evolutionarily conserved and structurally related to the DNA repair enzyme photolyase [2].
• Irradiation with blue light relieves this repression, presumably through an intra- or intermolecular redox reaction mediated through the flavin bound to the N-terminal photolyase-like domain [3].
• Two types of photolyase are known, one specific for cyclobutane pyrimidine dimers (CPD photolyase) and another specific for pyrimidine (6-4) pyrimidone photoproducts[(6-4)photolyase] [4].
• Similarity among the Drosophila (6-4)photolyase, a human photolyase homolog, and the DNA photolyase-blue-light photoreceptor family [4].
• Ultraviolet light (UV)-induced DNA damage can be repaired by DNA photolyase in a light-dependent manner [4].

Biological context of phr6-4

• Molecular evolution of the photolyase-blue-light photoreceptor family [5].
• We have now identified a third gene in Drosophila melanogaster with extensive sequence homology to the photolyase gene [6].

Associations of phr6-4 with chemical compounds

• The structure reveals a fold that is very similar to photolyase, with a single molecule of FAD noncovalently bound to the protein [7].
• BACKGROUND: Cryptochromes (CRY), members of the DNA photolyase/cryptochrome protein family, regulate the circadian clock in animals and plants [8].

References