Intrinsic nucleoside diphosphate kinase-like activity as a novel function of 14-3-3 proteins.
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 tau isoform exhibited intrinsic nucleoside diphosphate (NDP) kinase-like activity. 14-3-3 proteins preferentially catalyzed the transfer of the gamma-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.
Yano
M
M
Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, Japan.
Mori
S
S
Niwa
Y
Y
Inoue
M
M
Kido
H
H
D048948:14-3-3 Proteins; D006801:Humans; D006868:Hydrolysis; D016399:Lymphoma, T-Cell / Q000378:metabolism; D009701:Nucleoside-Diphosphate Kinase / Q000235:genetics / Q000378:metabolism*; D010766:Phosphorylation; D011506:Proteins / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D014407:Tumor Cells, Cultured; D014446:Tyrosine 3-Monooxygenase
D048948:14-3-3 Proteins; D011506:Proteins; D011994:Recombinant Proteins; D014446:Tyrosine 3-Monooxygenase; D009701:Nucleoside-Diphosphate Kinase