An unusual guanyl oligonucleotide regulates cellulose synthesis in Acetobacter xylinum

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Abstract
The mechanism of GTP‐specific activation of the mebrane‐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 Ca2+. It is suggested that the interaction between these enzymes and nucleotide derivatives, mediated by Ca2+, may regulate cellulose synthesis in vivo.