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Papers In Press, published online ahead of print January 14, 2003
UPR9073, Institut de Biologie Physico-chimique, Paris 75005
Corresponding Author: plumbridge{at}ibpc.fr
Mlc is a global regulator acting as a transcriptional repressor for several genes and operons of Escherichia coli encoding sugar-metabolizing enzymes and uptake systems. The repressing activity of Mlc is inactivated by binding to the dephosphorylated form of EIICBGlc (PtsG) which is formed during the transport of glucose. Here, we demonstrate that EIIBGlc, the cytoplasmic domain of PtsG, alone is sufficient to inactivate Mlc but only when EIIBGlc is attached to the membrane by a protein anchor, which can be unrelated to PtsG. Several EIIBGlc mutants, that were altered in and around the phosphorylation site (Cys421) of EIIBGlc, were tested for their ability to bind Mlc and to affect transcriptional repression by Mlc. The exchange of Cys421 with serine or aspartate still allowed binding to Mlc and in addition derepression became constitutive, i.e. independent of PTS phosphorylation. Mutations were made in the surface exposed residues in the vicinity of Cys421 and identified Arg424 as essential for binding to Mlc. Binding of Mlc to the EIIBGlc constructs in membrane preparations paralleled their ability to derepress Mlc-dependent transcription in vivo. These observations demonstrate that it is not the charge change at Cys421, produced by PTS phosphorylation, that allows Mlc binding but rather the structural change in the environment surrounding Cys421 that the phosphorylation provokes. Native Mlc exists as a tetramer. Deleting 18 amino acids from the C-terminal removes a putative amphipathic helix and results in dimeric Mlc which is no longer able to repress.
J. Biol. Chem, 10.1074/jbc.M212066200
Submitted on November 26, 2002
Revised on January 14, 2003
Accepted on January 14, 2003
Analysis of the interaction between the global regulator Mlc and EIIBGlc of the glucose-specific phosphotransferase system in Escherichia coli
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