A high-conductance mode of a poly-3-hydroxybutyrate/calcium/polyphosphate channel isolated from competent Escherichia coli cells

FEBS Lett. 2005 Sep 26;579(23):5187-92. doi: 10.1016/j.febslet.2005.08.032.


Reconstitution into planar lipid bilayers of a poly-3-hydroxybutyrate/calcium/polyphosphate (PHB/Ca(2+)/polyP) complex from Escherichia coli membranes yields cationic-selective, 100 pS channels (Das, S., Lengweiler, U.D., Seebach, D. and Reusch, R.N. (1997) Proof for a non-proteinaceous calcium-selective channel in Escherichia coli by total synthesis from (R)-3-hydroxybutanoic acid and inorganic polyphosphate. Proc. Natl. Acad. Sci. USA 94, 9075-9079). Here, we report that this complex can also form larger, weakly selective pores, with a maximal conductance ranging from 250pS to 1nS in different experiments (symmetric 150mM KCl). Single channels were inhibited by lanthanum (IC(50)=42+/-4microM, means+/-S.E.M.) with an unusually high Hill coefficient (8.4+/-1.2). Transition to low-conductance states (<250pS) was favored by increased membrane polarization (/V/ >or=50mV). High conductance states (>250pS) may reflect conformations important for genetic transformability, or "competence", of the bacterial cells, which requires the presence of the PHB/Ca(2+)/polyP complex in the membrane.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium / metabolism*
  • Calcium Channels / metabolism*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / metabolism*
  • Hydroxybutyrates / metabolism*
  • Ion Channel Gating
  • Lanthanum / metabolism
  • Lipid Bilayers
  • Membrane Potentials
  • Multiprotein Complexes
  • Patch-Clamp Techniques
  • Polyesters / metabolism*
  • Polyphosphates / chemistry
  • Polyphosphates / metabolism*


  • Calcium Channels
  • Escherichia coli Proteins
  • Hydroxybutyrates
  • Lipid Bilayers
  • Multiprotein Complexes
  • Polyesters
  • Polyphosphates
  • poly-beta-hydroxybutyrate
  • Lanthanum
  • Calcium