Format

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

1
Department of Biologlcal Chemistry, Institute of Life Sciences, The Hebrew Universty of Jerusalem, 91904 Jerusalem, Israel.

Abstract

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.

PMID:
19160595
DOI:
10.1016/0014-5793(85)80706-7
Free full text

LinkOut - more resources

Full Text Sources

Other Literature Sources

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center