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 (K D 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.
References
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 11:03 a.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 6:09 a.m.) |
Indexed | 1 year, 2 months ago (June 19, 2024, 5:48 a.m.) |
Issued | 27 years, 10 months ago (Oct. 20, 1997) |
Published | 27 years, 10 months ago (Oct. 20, 1997) |
Published Online | 27 years, 9 months ago (Nov. 25, 1997) |
Published Print | 27 years, 10 months ago (Oct. 20, 1997) |
@article{Weinhouse_1997, title={c‐di‐GMP‐binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum}, volume={416}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(97)01202-7}, DOI={10.1016/s0014-5793(97)01202-7}, number={2}, journal={FEBS Letters}, publisher={Wiley}, author={Weinhouse, Haim and Sapir, Shai and Amikam, Dorit and Shilo, Yehudit and Volman, Gail and Ohana, Patricia and Benziman, Moshe}, year={1997}, month=oct, pages={207–211} }