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Intrinsic nucleoside diphosphate kinase‐like activity as a novel function of 14‐3‐3 proteins
Author(s) -
Yano Mihiro,
Mori Sachie,
Niwa Yasuharu,
Inoue Masahiro,
Kido Hiroshi
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01469-5
Subject(s) - nucleoside diphosphate kinase , adenylate kinase , biochemistry , nucleoside , kinase , chemistry , nucleoside triphosphate , atp hydrolysis , adenosine triphosphate , enzyme , microbiology and biotechnology , biology , nucleotide , atpase , gene
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.