| Literature DB >> 9369216 |
H Weinhouse1, S Sapir, D Amikam, Y Shilo, G Volman, P Ohana, M Benziman.
Abstract
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.Entities:
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Year: 1997 PMID: 9369216 DOI: 10.1016/s0014-5793(97)01202-7
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124