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

• 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

書誌事項

タイトル別名

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

抄録

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 K_m values for the second substrate, ADP, than for the first substrate, NTP, and showed lowest and highest K_m values for GTP and CTP respectively.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 75 (9), 1740-1745, 2011

  公益社団法人 日本農芸化学会

キーワード

• nucleoside diphosphate kinase
• subcellular localization
• ping-pong mechanism
• gene expression
• enzyme characteristics

詳細情報

• CRID: 1390282681457118976
• NII論文ID: 10029757211
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.110285
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 11252749
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I11252749
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.110285
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可