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Single Amino Acid Substitution Reveals Latent Photolyase Activity in Arabidopsis cry1
Author(s) -
Burney Sarah,
Wenzel Ringo,
Kottke Tilman,
Roussel Thomas,
Hoang Nathalie,
Bouly JeanPierre,
Bittl Robert,
Heberle Joachim,
Ahmad Margaret
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201203476
Subject(s) - photolyase , cryptochrome , arabidopsis , flavin group , mutant , arabidopsis thaliana , biology , dna , computational biology , genetics , gene , dna repair , biochemistry , enzyme , circadian clock
A quick switch : A single amino acid substitution at a conserved residue (D396N) of Arabidopsis cryptochrome‐1 (Atcry1) confers single‐stranded DNA repair activity in vitro, conferring photolyase activity onto the cryptochrome (see graph). The mutant protein undergoes photoreduction of flavin to the fully reduced anionic form, similar to photolyases and unlike wild‐type cryptochromes.