Studies on phosphorylated transcriptional regulator (NarL) for E. coli nar operon by 31P-NMR spectroscopy

K. Takahashi, T. Hattori, H. Shindo, S. Noji, T. Nohno, S. Taniguchi

Research output: Contribution to journalArticlepeer-review

Abstract

The sequential transphosphorylation from autophosphorylated nitrate-sensing protein (NarX) to the transcriptional regulator protein (NarL), both operating in signal transduction to control the expression of the respiratory nitrate reductase (nar) operon in E. coli, was demonstrated with an in vitro reconstructed system to function similarly to other bacterial two-component regulatory systems. Over-expression system established by means of the pT7 promoter/polymerase provided both NarX and NarL proteins to reconstruct the in vitro transphosphorylation system. The phosphorylated NarL was detected, and the unstable phosphorylated group was directly assigned to acyl phosphate in the in vitro system by 31P-NMR spectroscopy.

Original languageEnglish
Pages (from-to)161-168
Number of pages8
JournalBiochemistry and Molecular Biology International
Volume31
Issue number1
Publication statusPublished - 1993

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics

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