Identification of a phosphorylation site in cyclobutane pyrimidine dimer photolyase of rice

Mika Teranishi, Kentaro Nakamura, Haruya Furukawa, Jun Hidema

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)

    Abstract

    Cyclobutane pyrimidine dimer (CPD) photolyase monomerises ultraviolet (UV) radiation-induced CPDs present in DNA, using energy from UVA and visible light. In plants, CPD photolyase activity is a crucial factor for determining UVB sensitivity. We previously demonstrated that native rice CPD photolyase is phosphorylated. To determine the phosphorylation site(s), the phosphorylation status of CPD photolyase was analyzed in rice varieties that have amino acid alterations at the potential phosphorylation sites. In wild-rice species, CPD photolyase was phosphorylated. In Poaceae species, CPD photolyase was phosphorylated in wheat but not in maize. Mutant CPD photolyase proteins, in which these putative phosphorylated residues were replaced with alanine residues, were synthesized using an insect cell-free translation system. A slow-migrating band disappeared when the serine residue at position 7 was mutated. A phospho-specific antibody was generated to determine whether this residue is phosphorylated in CPD photolyase. Only the slow-migrating band of native rice CPD photolyase was detected using this antibody, indicating that the serine residue at position 7 is a phosphorylation site in native rice CPD photolyase.

    Original languageEnglish
    Pages (from-to)24-29
    Number of pages6
    JournalPlant Physiology and Biochemistry
    Volume63
    DOIs
    Publication statusPublished - 2013 Feb

    Keywords

    • CPD photolyase
    • Cyclobutane pyrimidine dimers
    • Phosphorylation
    • Rice

    ASJC Scopus subject areas

    • Physiology
    • Genetics
    • Plant Science

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