c-di-GMP-binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum

FEBS Lett. 1997 Oct 20;416(2):207-11. doi: 10.1016/s0014-5793(97)01202-7.


A protein which specifically binds cyclic diguanylic acid (c-di-GMP), the reversible allosteric activator of the membrane-bound cellulose synthase system of Acetobacter xylinum, has been identified in membrane preparations of this organism. c-di-GMP binding is of high affinity (KD 20 nM), saturable and reversible. The equilibrium of the reaction is markedly and specifically shifted towards the binding direction by K+. The c-di-GMP binding protein, structurally associated with the cellulose synthase, appears to play a major role in modulating the intracellular concentration of free c-di-GMP and thus may constitute an essential factor in regulating cellulose synthesis in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allosteric Regulation
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / metabolism*
  • Cellulose / biosynthesis*
  • Chromatography, Gel
  • Cyclic GMP / analogs & derivatives*
  • Cyclic GMP / metabolism
  • Energy Metabolism / drug effects
  • Enzyme Activation
  • Ethanolamines / pharmacology
  • Gluconacetobacter xylinus / metabolism*
  • Glucosyltransferases / metabolism
  • Kinetics
  • Potassium / pharmacology


  • Bacterial Proteins
  • Carrier Proteins
  • Ethanolamines
  • bis(3',5')-cyclic diguanylic acid
  • Cellulose
  • diethanolamine
  • Glucosyltransferases
  • cellulose synthase (cyclic diguanylic acid)
  • Cyclic GMP
  • Potassium