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PMID: 9369216 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 416 ·No. 2 ·1997-10-20 ·Pages 207-11

Weinhouse H, Sapir S, Amikam D, Shilo Y, Volman G, Ohana P, Benziman M

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.

MeSH Terms
Allosteric Regulation Bacterial Proteins/isolation & purification,metabolism Carrier Proteins/isolation & purification,metabolism Cellulose/biosynthesis Chromatography, Gel Cyclic GMP/analogs & derivatives,metabolism Energy Metabolism/drug effects Enzyme Activation Ethanolamines/pharmacology Gluconacetobacter xylinus/metabolism Glucosyltransferases/metabolism Kinetics Potassium/pharmacology
Chemicals
Bacterial Proteins Carrier Proteins Ethanolamines bis(3',5')-cyclic diguanylic acid Cellulose diethanolamine Glucosyltransferases cellulose synthase (cyclic diguanylic acid) Cyclic GMP Potassium
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Weinhouse H
Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, Givat Ram, Israel.
Sapir S
Amikam D
Shilo Y
Volman G
Ohana P
Benziman M
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1997-10-20
Pages
207-11
Language
English
Region
England
NLM ID
0155157
Subset
IM
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