Physiological and Biochemical Characterization of Three Nucleoside Diphosphate Kinase Isozymes from Rice (Oryza sativa L.)

DOI IR (HANDLE) HANDLE Web Site Web Site View 1 Remaining Hide 3 Citations 39 References Open Access
  • KIHARA Akihiko
    Laboratory of Biochemistry, Research Faculty of Agriculture, Hokkaido University
  • SABURI Wataru
    Laboratory of Biochemistry, Research Faculty of Agriculture, Hokkaido University
  • WAKUTA Shinji
    Laboratory of Biochemistry, Research Faculty of Agriculture, Hokkaido University
  • KIM Myung-Hee
    Crop Cold-Tolerance Research Team, National Agricultural Research Center for The Hokkaido Region
  • HAMADA Shigeki
    Laboratory of Biochemistry, Research Faculty of Agriculture, Hokkaido University
  • ITO Hiroyuki
    Laboratory of Biochemistry, Research Faculty of Agriculture, Hokkaido University
  • IMAI Ryozo
    Crop Cold-Tolerance Research Team, National Agricultural Research Center for The Hokkaido Region
  • MATSUI Hirokazu
    Laboratory of Biochemistry, Research Faculty of Agriculture, Hokkaido University

Bibliographic Information

Other Title
  • Physiological and Biochemical Characterization of Three Nucleoside Diphosphate Kinase Isozymes from Rice (<i>Oryza sativa</i>L.)

Search this article

Description

Nucleoside diphosphate kinase (NDPK) is a ubiquitous enzyme that catalyzes the transfer of the γ-phosphoryl group from a nucleoside triphosphate to a nucleoside diphosphate. In this study, we examined the subcellular localization, tissue-specific gene expression, and enzymatic characteristics of three rice NDPK isozymes (OsNDPK1-OsNDPK3). Sequence comparison of the three OsNDPKs suggested differential subcellular localization. Transient expression of green fluorescence protein-fused proteins in onion cells indicated that OsNDPK2 and OsNDPK3 are localized to plastid and mitochondria respectively, while OsNDPK1 is localized to the cytosol. Expression analysis indicated that all the OsNDPKs are expressed in the leaf, leaf sheath, and immature seeds, except for OsNDPK1, in the leaf sheath. Recombinant OsNDPK2 and OsNDPK3 showed lower optimum pH and higher stability under acidic pH than OsNDPK1. In ATP formation, all the OsNDPKs displayed lower Km values for the second substrate, ADP, than for the first substrate, NTP, and showed lowest and highest Km values for GTP and CTP respectively.

Journal

Citations (3)*help

See more

References(39)*help

See more

Details 詳細情報について

Report a problem

Back to top