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Catabolite control of Escherichia coli regulatory protein BglG activity by antagonistically acting phosphorylations
Author(s) -
Görke Boris,
Rak Bodo
Publication year - 1999
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/18.12.3370
Subject(s) - catabolite repression , biology , escherichia coli , escherichia coli proteins , biochemistry , microbiology and biotechnology , gene , mutant
In bacteria various sugars are taken up and concomitantly phosphorylated by sugar‐specific enzymes II (EII) of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). The phosphoryl groups are donated by the phosphocarrier protein HPr. BglG, the positively acting regulatory protein of the Escherichia coli bgl (β‐glucoside utilization) operon, is known to be negatively regulated by reversible phosphorylation catalyzed by the membrane spanning β‐glucoside‐specific EII Bgl . Here we present evidence that in addition BglG must be phosphorylated by HPr at a distinct site to gain activity. Our data suggest that this second, shortcut route of phosphorylation is used to monitor the state of the various PTS sugar availabilities in order to hierarchically tune expression of the bgl operon in a physiologically meaningful way. Thus, the PTS may represent a highly integrated signal transduction network in carbon catabolite control.