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      Translocation of N-terminal tails across the plasma membrane.

      The EMBO Journal
      Adenosine Triphosphatases, physiology, Amino Acid Sequence, Bacterial Proteins, Biological Transport, Capsid, metabolism, Capsid Proteins, Electrophysiology, Endopeptidases, Escherichia coli, Escherichia coli Proteins, Membrane Proteins, Membrane Transport Proteins, Molecular Sequence Data, Protein Conformation, Protein Sorting Signals, Recombinant Fusion Proteins, Serine Endopeptidases, Structure-Activity Relationship

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          Abstract

          Previously we have shown that the first hydrophobic domain of leader peptidase (lep) can function to translocate a short N-terminal 18 residue antigenic peptide from the phage Pf3 coat protein across the plasma membrane of Escherichia coli. We have now examined the mechanism of insertion of N-terminal periplasmic tails and have defined the features needed to translocate these regions. We find that short tails of up to 38 residues are efficiently translocated in a SecA- and SecY-independent manner while longer tails are very poorly inserted. Efficient translocation of a 138 residue tail is restored and is Sec-dependent by the addition of a leader sequence to the N-terminus of the protein. We also find that while there is no amphiphilic helix requirement for N-terminal translocation, there is a charge requirement that is needed within the tail; an arginine and lysine residue can inhibit or completely block translocation when introduced into the tail region. Intriguingly, the membrane potential is required for insertion of a 38 residue tail but not for a 23 residue tail.

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