1887

Abstract

The operon of consists of two adjacent genes, and , encoding glucose- and glucoside-specific enzymes II, respectively, the sugar permeases of the phosphoenolpyruvate-dependent phosphotransferase system (PTS). The expression of the operon is glucose-inducible. Putative RAT (ribonucleic antiterminator) and terminator sequences localized in the promoter region of suggest regulation via antitermination. The gene was cloned and the putative antiterminator protein GlcT was purified. Activity of this protein was demonstrated in and . studies led to the assumption that phosphoenolpyruvate-dependent phosphorylation of residue His105 via the general PTS components enzyme I and HPr facilitates dimerization of GlcT and consequently activation. Because of the high similarity of the two -RAT sequences of and , studies were performed in . These indicated that GlcT of is able to recognize -RAT sequences of and to cause antitermination. The specific interaction between -RAT and GlcT demonstrated by surface plasmon resonance suggests that only the dimer of GlcT binds to the RAT sequence. HPr-dependent phosphorylation of GlcT facilitates dimer formation and may be a control device for the proper function of the general PTS components enzyme I and HPr necessary for glucose uptake and phosphorylation by the corresponding enzyme II.

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2000-09-01
2024-04-23
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