A PUTATIVE MONOFUNCTIONAL GLYCOSYLTRANSFERASE IS EXPRESSED IN RALSTONIA-EUTROPHA

A gene, mgt, encoding a protein homologous to the N-terminal module of class A high-molecular-mass penicillin-binding proteins was identifie d in Ralstonia eutropha. By using specific antibodies, the correspondi ng Mgt protein was detected in association with the membrane, confirmi ng that the N-terminal hydrophobic segment functioned as a membrane an chor, A derivative in which the hydrophobic sequence was deleted was o verexpressed as a maltose-binding fusion protein in Escherichia coli. Cleavage of the product resulted in substantial amounts of soluble Mgt derivative, indicating that folding occurs independently on other pro teins or on homologous domains of penicillin-binding proteins.