Papers

Folia Microbiologica

, Volume 42, Issue 3, pp 179-183

First online:

Protein secretion by gram-negative bacterial ABC exporters

  • R. BinetAffiliated withUnité de Physiologie Cellulaire, Institut Pasteur, URA 1300, CNRS
  • , S. LétofféAffiliated withUnité de Physiologie Cellulaire, Institut Pasteur, URA 1300, CNRS
  • , J. M. GhigoAffiliated withUnité de Physiologie Cellulaire, Institut Pasteur, URA 1300, CNRS
  • , P. DelepelaireAffiliated withUnité de Physiologie Cellulaire, Institut Pasteur, URA 1300, CNRS
  • , C. WandersmanAffiliated withUnité de Physiologie Cellulaire, Institut Pasteur, URA 1300, CNRS

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Abstract

One of the strategies used by Gram-negative bacteria to secrete proteins across the two membranes which delimit the cells, issec independent and dedicated to proteins lacking an N-terminal signal peptide. It depends on ABC protein-mediated exporters, which consist of three cell envelope proteins: two inner membrane proteins: an ATPase (the ABC protein), a membrane fusion protein (MFP) and an outer membrane polypeptide.Erwinia chrysanthemi metalloproteinases B and C, andSerratia marcescens hemoprotein HasA are secreted by such homologous pathways and interact with the ABC protein. Interaction between the ABC protein and its substrate has also been evidenced by studies on proteinase and HasA hybrid transporters obtained by combining components from each system. Association between hemoprotein HasA and the three exporter/secretion proteins was demonstrated by affinity chromatography on hemin agarose on which the substrate remained bound with the three secretion proteins. The three component association was ordered and substrate binding was required for the formation of this multiprotein complex.