Intrinsic nucleoside diphosphate kinase‐like activity as a novel function of 14‐3‐3 proteins

FEBS Letters

Niwa, Yasuharu¹  Kido, Hiroshi¹  Yano, Mihiro¹  Inoue, Masahiro¹  Mori, Sachie¹ 

[1] Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Tokushima 770, Japan

关键词: 14-3-3;    Nucleoside diphosphate kinase;    ATP/ADP exchange;    Molecular chaperone;    ATPase;    NDP;    nucleoside diphosphate;    E. coli;    Escherichia coli;    Hsp;    heat shock protein;    AMP-PNP;    5′-adenylyl-β;    γ-imidodiphosphate;    ATPγS;    adenosine 5′-3-O-(thio)triphosphate;    TLC;    thin-layer chromatography;    BSA;    bovine serum albumin;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(97)01469-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

14-3-3 proteins play a role in many cellular functions as molecular chaperone and adapter proteins: they bind to and modulate several proteins involved in cell proliferation and differentiation, and also function ATP-dependently in targeting of precursors to mitochondria. We show here that 14-3-3 purified from a human lymphoblastoma and also its recombinant τ isoform exhibited intrinsic nucleoside diphosphate (NDP) kinase-like activity. 14-3-3 proteins preferentially catalyzed the transfer of the γ-phosphate group from ATP, dATP or dGTP to all nucleoside diphosphates and this transfer involved acid-labile phosphoenzyme intermediates. They also simultaneously catalyzed the reverse reaction of ATP hydrolysis. These properties of 14-3-3 are similar to those of NDP kinase, but not to those of adenylate kinase.

【 授权许可】

Unknown