The phosphoenolpyruvate-dependent glucose-phosphotransferase system from Escherichia coli K-12 as the center of a network regulating carbohydrate flux in the cell

Elisabeth Gabor, Anna Katharina Göhler, Anne Kosfeld, Ariane Staab, Andreas Kremling, Knut Jahreis

Research output: Contribution to journalShort surveypeer-review

52 Scopus citations

Abstract

The phosphoenolpyruvate-(PEP)-dependent-carbohydrate:phosphotransferase systems (PTSs) of enteric bacteria constitute a complex transport and sensory system. Such a PTS usually consists of two cytoplasmic energy-coupling proteins, Enzyme I (EI) and HPr, and one of more than 20 different carbohydrate-specific membrane proteins named Enzyme II (EII), which catalyze the uptake and concomitant phosphorylation of numerous carbohydrates. The most prominent representative is the glucose-PTS, which uses a PTS-typical phosphorylation cascade to transport and phosphorylate glucose. All components of the glucose-PTS interact with a large number of non-PTS proteins to regulate the carbohydrate flux in the bacterial cell. Several aspects of the glucose-PTS have been intensively investigated in various research projects of many groups. In this article we will review our recent findings on a Glc-PTS-dependent metalloprotease, on the interaction of EIICB Glc with the regulatory peptide SgrT, on the structure of the membrane spanning C-domain of the glucose transporter and on the modeling approaches of ptsG regulation, respectively, and discuss them in context of general PTS research.

Original languageEnglish
Pages (from-to)711-720
Number of pages10
JournalEuropean Journal of Cell Biology
Volume90
Issue number9
DOIs
StatePublished - Sep 2011

Keywords

  • Bacterial phosphotransferase system
  • Carbohydrate transport
  • Catabolite repression
  • Gene regulation
  • Glucose
  • Integral membrane protein
  • Metabolic balance
  • Mlc
  • Modeling
  • MtfA
  • PTS
  • PtsG
  • SgrT

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