Structure and molecular characterization of barley nudix hydrolase genes

Sayuri Tanaka, Makoto Kihara, Manabu Sugimoto

    Research output: Contribution to journalArticlepeer-review

    3 Citations (Scopus)

    Abstract

    Putative nudix hydrolase (NUDX) genes, which encode amino acid sequences showing homology with those of Arabidopsis NUDXs and conserve nudix motif, were identified from barley. The 14 deduced barley NUDXs (HvNUDX1-14) were classified into established subfamilies, except for 8-oxo-deoxyguanosine 5′-triphosphate (8-oxo-dGTP) pyrophosphohydrolase and mRNA decapping enzyme subfamilies, and three substrate-unknown subfamilies. Drought and UV-C stresses, respectively, up-regulated 7 and 4 HvNUDX genes, but some homologs of Arabidopsis NUDXs showed different responses to abiotic stress. HvNUDX12 gene, belonging to diadenosine tetraphosphates (Ap4A) pyrophosphohydrolase subfamily gene and up-regulated by UV-C, was expressed in Escherichia coli cells. The recombinant protein showed 8-oxo-dGTP, Ap4A, and guanosine-3′,5′-tetraphosphate (ppGpp) pyrophosphohydrolase activities, and the suppression of the lacZ amber mutation in a mutT-deficient E. coli cells caused by the incorporation of 8-oxo-GTP into mRNA was prevented to a significant degree. These results suggest that barley NUDXs have unique constitution and response of NUDX to abiotic stress.

    Original languageEnglish
    Pages (from-to)394-401
    Number of pages8
    JournalBioscience, Biotechnology and Biochemistry
    Volume79
    Issue number3
    DOIs
    Publication statusPublished - 2015

    Keywords

    • 8-oxo-dGTP
    • Abiotic stress
    • Barley
    • Nudix hydrolase
    • UV-C

    ASJC Scopus subject areas

    • Biotechnology
    • Analytical Chemistry
    • Biochemistry
    • Applied Microbiology and Biotechnology
    • Molecular Biology
    • Organic Chemistry

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