Send to

Choose Destination
FEBS Lett. 1985 Jul 8;186(2):191-6.

An unusual guanyl oligonucleotide regulates cellulose synthesis in Acetobacter xylinum.

Author information

Department of Biologlcal Chemistry, Institute of Life Sciences, The Hebrew Universty of Jerusalem, 91904 Jerusalem, Israel.


The mechanism of GTP-specific activation of the membrane-bound cellulose synthase system of Acetobacter xylinum has been further elucidated. The supernatant fraction derived from washed membranes of this organism contains an enzyme which reacts with GTP to form a low molecular mass, heat-stable compound,tentatively characterized as a cyclic oligonuleotide composed of GMP residues, which is the immediate activator of the cellulose synthase. This activation is reversed by a membrane-bound enzyme that degrades the activator; the latter enzyme is inhibited by Ca (2+). It is suggested that the interaction between these enzymes and nucleotide derivatives, mediated by Ca (2+), may regulate cellulose synthesis in VIVO.

Free full text

LinkOut - more resources

Full Text Sources

Other Literature Sources

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center