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

Mihiro Yano, Sachie Mori, Yasuharu Niwa, Masahiro Inoue, Hiroshi Kido

Research output: Contribution to journalArticlepeer-review

13 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)244-248
Number of pages5
JournalFEBS Letters
Volume419
Issue number2-3
DOIs
Publication statusPublished - 15-12-1997
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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