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c-di-GMP-binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum
H Weinhouse1, S Sapir, D Amikam
1Department of Biological Chemistry, Institute of Life Sciences, Hebrew University of Jerusalem, Givat Ram, Israel.
FEBS Letters
|November 22, 1997
Summary
Researchers identified a protein that binds cyclic diguanylic acid (c-di-GMP), a key activator of cellulose synthesis in Acetobacter xylinum. This protein regulates c-di-GMP levels, controlling cellulose production.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Acetobacter xylinum synthesizes cellulose via a membrane-bound system.
- Cellulose synthesis is regulated by intracellular cyclic diguanylic acid (c-di-GMP).
- c-di-GMP acts as an allosteric activator for the cellulose synthase complex.
Purpose of the Study:
- To identify and characterize the protein responsible for binding c-di-GMP in Acetobacter xylinum.
- To elucidate the role of this protein in regulating cellulose synthesis.
Main Methods:
- Isolation of membrane preparations from Acetobacter xylinum.
- Characterization of c-di-GMP binding to the identified protein using binding assays.
- Assessment of the protein's association with the cellulose synthase system.
Main Results:
- A high-affinity (KD 20 nM), saturable, and reversible c-di-GMP binding protein was identified.
- Potassium ions (K+) specifically and markedly shifted the binding equilibrium towards the protein.
- The c-di-GMP binding protein is structurally associated with the cellulose synthase.
Conclusions:
- The identified protein plays a crucial role in modulating intracellular free c-di-GMP concentrations.
- This protein is likely an essential regulator of cellulose synthesis in Acetobacter xylinum.
- Understanding this regulatory mechanism offers insights into bacterial cellulose production.