Discrimination of class I cyclobutane pyrimidine dimer photolyase from blue light photoreceptors by single methionine residue.

ABSTRACT: DNA photolyase recognizes ultraviolet-damaged DNA and breaks improperly formed covalent bonds within the cyclobutane pyrimidine dimer by a light-activated electron transfer reaction between the flavin adenine dinucleotide, the electron donor, and cyclobutane pyrimidine dimer, the electron acceptor. Theoretical analysis of the electron-tunneling pathways of the DNA photolyase derived from Anacystis nidulans can reveal the active role of the protein environment in the electron transfer reaction. Here, we report the unexpectedly important role of the single methionine residue, Met-353, where busy trafficking of electron-tunneling currents is observed. The amino acid conservation pattern of Met-353 in the homologous sequences perfectly correlates with experimentally verified annotation as phot

SUBMITTER: Miyazawa Y 

PROVIDER: S-EPMC2257881 | biostudies-literature | 2008 Mar

REPOSITORIES: biostudies-literature