The gene for nucleoside diphosphate kinase functions as a mutator gene in Escherichia coli

Qing Lu, Xiaolin Zhang, Niva Almaula, Christopher K. Mathews, Masayori Inouye

Research output: Contribution to journalEditorialpeer-review

95 Scopus citations


Nucleoside diphosphate (NDP) kinase is a key enzyme in the control of cellular concentrations of nucleoside triphosphates, and has been shown to play important roles in various cellular activities such as developmental control, signal transduction and metastasis in eukaryotic systems. In this study, the gene for NDP kinase of Escherichia coli (ndk) was disrupted and surprisingly found to be dispensable without any discernible effects on cell growth or morphology. However, a mutator phenotype was found in ndk-disruption strains; frequencies of spontaneous mutations to rifampicin resistance and nalidixic acid resistant significantly increased. A higher frequency in reversion mutations was observed with use of an amber mutation in the kanamycin-resistance gene in an ndk-disruption strain. Imbalance in dNTP pools, in particular a significant increase of the dCTP content was observed, which is likely to result in the higher spontaneous mutation rates. These results suggest that NDP kinase, although not essential, plays an important role in the appropriate balance of intracellular dNTP pools to maintain a high DNA replication fidelity. Strains with ndk- pykA- pykF- as well as ndk - scs - were constructed without any discernible effect on cell growth, indicating that there is yet another enzyme(s) catalyzing nucleoside triphosphate synthesis, in addition to NDP kinase, pyruvate kinases and succinyl CoA synthetase.

Original languageEnglish (US)
Pages (from-to)337-341
Number of pages5
JournalJournal of molecular biology
Issue number3
StatePublished - Dec 1 1995

All Science Journal Classification (ASJC) codes

  • Molecular Biology


  • Dntp pool
  • Mutator gene
  • Nucleoside diphosphate kinase
  • Pyruvate kinases
  • Succinyl CoA synthetase

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