Spatial and temporal organization of the E. coli PTS components

Livnat Lopian, Yair Elisha, Anat Nussbaum-Shochat, Orna Amster-Choder*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

39 Scopus citations


The phosphotransferase system (PTS) controls preferential use of sugars in bacteria. It comprises of two general proteins, enzyme I (EI) and HPr, and various sugar-specific permeases. Using fluorescence microscopy, we show here that EI and HPr localize near the Escherichia coli cell poles. Polar localization of each protein occurs independently, but HPr is released from the poles in an EI- and sugar-dependent manner. Conversely, the Î 2-glucoside-specific permease, BglF, localizes to the cell membrane. EI, HPr and BglF control the Î 2-glucoside utilization (bgl) operon by modulating the activity of the BglG transcription factor; BglF inactivates BglG by membrane sequestration and phosphorylation, whereas EI and HPr activate it by an unknown mechanism in response to Î 2-glucosides availability. Using biochemical, genetic and imaging methodologies, we show that EI and HPr interact with BglG and affect its subcellular localization in a phosphorylation-independent manner. Upon sugar stimulation, BglG migrates from the cell periphery to the cytoplasm through the poles. Hence, the PTS components appear to control bgl operon expression by ushering BglG between the cellular compartments. Our results reinforce the notion that signal transduction in bacteria involves dynamic localization of proteins.

Original languageAmerican English
Pages (from-to)3630-3645
Number of pages16
JournalEMBO Journal
Issue number21
StatePublished - 3 Nov 2010


  • bacterial polarity
  • bacterial sensory systems
  • cell poles
  • subcellular localization of proteins
  • transcription antitermination


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