Complex Formation Between AmtB and GlnK: An Ancestral Role in Prokaryotic Nitrogen Control

Biochem Soc Trans. 2005 Feb;33(Pt 1):170-2. doi: 10.1042/BST0330170.

Abstract

Ammonium transport proteins belonging to the Amt family are ubiquitous in prokaryotes. In Escherichia coli, the AmtB protein and the associated P(II) signal transduction protein (GlnK) have recently been recognized as an ammonium sensory system that effectively couples the intracellular nitrogen regulation (Ntr) system to external changes in ammonium availability. Given the almost invariant coupling of AmtB and GlnK in bacteria and archaea it seems probable that these two proteins may constitute an ancestral nitrogen-responsive system that has been coupled with a variety of unrelated nitrogen regulatory processes, which are now found in prokaryotes. The multiplicity of P(II) proteins could therefore be considered to have evolved from an ancestral GlnK-like protein and to have subsequently been adapted to control many other aspects of nitrogen metabolism.

MeSH terms

  • Bacteria / metabolism*
  • Bacterial Proteins / metabolism*
  • Cation Transport Proteins / metabolism*
  • Escherichia coli Proteins / metabolism*
  • Nitrogen / metabolism*
  • Operon

Substances

  • AmtB protein, E coli
  • Bacterial Proteins
  • Cation Transport Proteins
  • Escherichia coli Proteins
  • GlnK protein, Azorhizobium caulinodans
  • Nitrogen