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An unusual guanyl oligonucleotide regulates cellulose synthesis in Acetobacter xylinum
Author(s) -
Ross Peter,
Aloni Yehoshua,
Weinhouse Chaim,
Michaeli Dorit,
Weinberger-Ohana Patricia,
Meyer Raphael,
Benziman Moshe
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80706-7
Subject(s) - gtp' , enzyme , biochemistry , activator (genetics) , chemistry , cellulose , atp synthase , membrane , acetobacter , nucleotide , oligonucleotide , fermentation , gene
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 Ca 2+ . It is suggested that the interaction between these enzymes and nucleotide derivatives, mediated by Ca 2+ , may regulate cellulose synthesis in vivo.