title: An unusual guanyl oligonucleotide regulates cellulose synthesis in Acetobacter xylinum.
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.
authors.affiliation: Department of Biologlcal Chemistry, Institute of Life Sciences, The Hebrew Universty of Jerusalem, 91904 Jerusalem, Israel.
authors.forename: P
authors.initials: P
authors.lastname: Ross
authors.forename: Y
authors.initials: Y
authors.lastname: Aloni
authors.forename: C
authors.initials: C
authors.lastname: Weinhouse
authors.forename: D
authors.initials: D
authors.lastname: Michaeli
authors.forename: P
authors.initials: P
authors.lastname: Weinberger-Ohana
authors.forename: R
authors.initials: R
authors.lastname: Meyer
authors.forename: M
authors.initials: M
authors.lastname: Benziman