Structure-function relationships of DNA photolyase: Analysis of electron transfer reaction

DOI

Bibliographic Information

Other Title
  • DNAフォトリアーゼの構造―機能相関～電子移動反応の解析～

Description

DNA photolyase recognizes UV-damaged DNA and breaks improperly formed covalent bonds within the cyclobutane pyrimidine dimer (CPD) by light-activated electron transfer reaction between the flavin adenine dinucleotide, the electron donor, and CPD, 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 photolyases. The bioinformatics sequence analysis also suggests that the residue plays a pivotal role in biological function. Consistent findings from different disciplines of computational biology strongly suggest the pivotal role of Met-353 in the biological function of DNA photolyase.

Journal

Details 詳細情報について

  • CRID
    1390001205631531136
  • NII Article ID
    130006992781
  • DOI
    10.14841/jspp.2009.0.s0026.0
  • Data Source
    • JaLC
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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