PMID:15760712

Citation	Pradel, N, Decorps, A, Ye, C, Santini, CL and Wu, LF (2005) YidC-dependent translocation of green fluorescence protein fused to the FliP cleavable signal peptide. Biochimie 87:191-6
Abstract	Escherichia coli FliP is a rare bacterial polytopic membrane protein synthesized with a cleavable, highly hydrophobic signal peptide. More hydrophilic Tat-dependent or Sec-dependent signal peptide is functionally capable of substituting for the FliP signal peptide, but a signal anchor of inner membrane protein fails to do so. To assess the intrinsic characteristics of the FliP signal peptide in mediating protein translocation, we fused it to green fluorescence protein and observed that the translocation of the chimera (FliPss-GFP) was dependent of Ffh, SecA, SecY and SecD. In addition, we showed for the first time the involvement of YidC in protein translocation across the inner membrane.
Links	PubMed Online version:10.1016/j.biochi.2004.11.001
Keywords	Escherichia coli/genetics; Escherichia coli/physiology; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Green Fluorescent Proteins/genetics; Green Fluorescent Proteins/metabolism; Membrane Proteins/genetics; Membrane Transport Proteins/genetics; Membrane Transport Proteins/metabolism; Protein Sorting Signals/genetics; Protein Sorting Signals/physiology; Protein Transport/genetics; Protein Transport/physiology; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism
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