BglF, the sensor of the E.coli bgl system, uses the same site to phosphorylate both a sugar and a regulatory protein

Qing Chen, Jos C. Arents, Rechien Bader, Pieter W. Postma, Orna Amster-Choder*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

The Escherichia coli BglF protein is a sugar permease that is a member of the phosphoenolpyruvate-dependent phosphotransferase system (PTS). It catalyses transport and phosphorylation of β-glucosides. In addition to its ability to phosphorylate its sugar substrate, BglF has the unusual ability to phosphorylate and dephosphorylate the transcriptional regulator BglG according to β-glucoside availability. By controlling the phosphorylation state of BglG, BglF controls the dimeric state of BglG and thus its ability to bind RNA and antiterminate transcription of the bgl operon. BglF has two phosphorylation sites. The first site accepts a phosphoryl group from the PTS protein HPr; the phosphoryl group is then transferred to the second phosphorylation site, which can deliver it to the sugar. We provide both in vitro and in vivo evidence that the same phosphorylation site on BglF, the second one, is in charge not only of sugar phosphorylation but also of BglG phosphorylation. Possible mechanisms that ensure correct phosphoryl delivery to the right entity, sugar or protein, depending on environmental conditions, are discussed.

Original languageAmerican English
Pages (from-to)4617-4627
Number of pages11
JournalEMBO Journal
Volume16
Issue number15
DOIs
StatePublished - 1 Aug 1997

Keywords

  • Bgl system
  • PTS
  • Phosphorylation sites
  • Protein phosphorylation
  • β-glucosides

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