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. 2018 Oct 29;293(51):19919–19931. doi: 10.1074/jbc.RA118.005548

Figure 1.

Figure 1.

A, thematic representation of the dual-substrate accessing mechanism of LplT in the bacterial inner membrane. LplT recruits LPL substrates (1) from the outer leaflet of the inner membrane generated by Lnt or (2) from the periplasmic space to flip them across the bilayer to the inner leaflet, which are then acylated by Aas to form diacyl lipids on the cytoplasmic surface. B, TLC image of the total phospholipids extracted from spheroplasts generated from E. coli BL21(DE3) ΔlplT cells expressing LplTKp WT. C, Western blotting of Lpp in E. coli Trp-3110 WT, ΔlplT, and Δaas, and PAP9502 strains using anti-Lpp antibody. The conditional lnt gene knockout strain PAP9502 was grown in the depleted condition (+glucose) or rescuing condition (+arabinose). The same amount of protein was loaded in each lane. D, [32P]LPE transport assays of LplTKp using spheroplasts prepared from E. coli BL21(DE3) Δaas-lplT strain expressing LplTKp WT (black squares) and vector only (open circles) or vector only inside-out vesicles (ISO, open triangles). Radioactivity counts were directly used to calculate the transport activity.