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. 2022 Jan 17;41(5):e109800. doi: 10.15252/embj.2021109800

Figure 6. Partitioning of membrane proteins into fluid domains of phase‐separated plasma membranes.

Figure 6

  1. Time lapse images of E. coli fabA(Ts) cells expressing FOF1 a‐mNG. For corresponding controls, see Appendix Fig S10. Cells were grown at 30°C and shifted from 30°C to non‐permissive 37°C. See Movie EV2 for full time lapse.
  2. Images of E. coli fabA(Ts) co‐expressing WALP23‐mScarlet‐I and FOF1 a‐mNG grown at permissive 30°C or shifted to non‐permissive 40°C. For fluorescence intensity correlations, see Appendix Fig S8D. For corresponding images of E. coli fabA(Ts) cells co‐expressing inner membrane marker FOF1 a‐mNG and outer membrane marker OmpA‐mCherry, see Fig EV5.
  3. Images of FOF1 a‐mCherry‐expressing E. coli fabA(Ts) grown at 30°C or shifted to non‐permissive 37°C and stained with Laurdan. For fluorescence intensity correlations, see Appendix Fig S8E.
  4. Growth behaviour of FOF1 a‐mNG expressing E. coli fabA(Ts) after shift from 30°C to non‐permissive 37°C and upon recovery through exogenous supplementation with UFA oleate (cis‐Δ9‐C18:1). The corresponding reversible segregation of FOF1 a‐mNG is shown above the growth curve. For further controls, see Appendix Fig S11A. For a comparable fluorescence time lapse analysis of mNG‐labelled glucose permease PtsG, see Appendix Fig S12.
  5. Fatty acid composition of E. coli fabA(Ts) cells (same cell batch as in D) upon growth at 30°C, upon depletion of UFA by incubation at 37°C for 120 min and upon recovery by oleate supplementation for additional 120 min. For detailed analyses, see Appendix Fig S11B–D.

Data information: (A–D) The experiments are representative of biological triplicates. (E) The histogram depicts mean and SD of biological triplicates. DIC, differential interference contrast. Scale bar: (A, B, D) 2 µm; (C) 3 µm. Strains used: (A, D, E) E. coli MG4; (B), E. coli MG4/pBH501; (C), E. coli LF6.red.

Source data are available online for this figure.