Reconstitution of functionally efficient SecA-dependent protein-conducting channels: transformation of low-affinity SecA-liposome channels to high-affinity SecA-SecYEG-SecDF·YajC channels

Biochem Biophys Res Commun. 2013 Feb 15;431(3):388-92. doi: 10.1016/j.bbrc.2013.01.042. Epub 2013 Jan 18.

Abstract

Previous work showed that SecA alone can promote protein translocation and ion-channel activity in liposomes, and that SecYEG increases efficiency as well as signal peptide specificity. We now report that SecDF·YajC further increases translocation and ion-channel activity. These activities of reconstituted SecA-SecYEG-SecDF·YajC-liposome are almost the same as those of native membranes, indicating the transformation of reconstituted functional high-affinity protein-conducting channels from the low-affinity SecA-channels.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / metabolism*
  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism*
  • Ion Channels / chemistry
  • Ion Channels / metabolism*
  • Liposomes / chemistry
  • Liposomes / metabolism*
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Membrane Transport Proteins / chemistry
  • Membrane Transport Proteins / metabolism*
  • Protein Transport
  • SEC Translocation Channels
  • SecA Proteins
  • Xenopus laevis

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Ion Channels
  • Liposomes
  • Membrane Proteins
  • Membrane Transport Proteins
  • SEC Translocation Channels
  • SecD protein, E coli
  • SecF protein, E coli
  • Adenosine Triphosphatases
  • SecA Proteins