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Protein secretion through autotransporter and two-partner pathways.

Françoise Jacob-Dubuisson1, Rachel Fernandez, Loic Coutte

  • 1INSERM U629, Institut de Biologie de Lille, Institut Pasteur de Lille, 1 rue Calmette, 59019 Lille Cedex, France. francoise.Jacob@pasteur-lille.fr <francoise.Jacob@pasteur-lille.fr>

Biochimica Et Biophysica Acta
|November 18, 2004
PubMed
Summary

The autotransporter (AT) and two-partner secretion (TPS) pathways are distinct Gram-negative bacterial protein secretion systems. Both utilize outer membrane porins for translocating large proteins, but differ in how specificity is achieved.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Bacterial Physiology

Background:

  • Gram-negative bacteria employ specialized protein secretion pathways to translocate proteins across their complex cell envelopes.
  • The autotransporter (AT) and two-partner secretion (TPS) pathways are two prominent systems for secreting large proteins or protein domains across the outer membrane.
  • Both pathways involve Sec-dependent translocation across the inner membrane followed by outer membrane passage mediated by cognate transporters.

Purpose of the Study:

  • To elucidate the mechanisms and compare the characteristics of the autotransporter (AT) and two-partner secretion (TPS) protein secretion pathways in Gram-negative bacteria.
  • To highlight the structural and functional differences between AT and TPS systems, particularly in achieving specificity.
  • To characterize the outer membrane porins involved in these secretion systems.

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Main Methods:

  • Comparative analysis of protein structures and secretion mechanisms.
  • Bioinformatic analysis of conserved domains and protein families.
  • Review of existing literature on AT and TPS pathway components and functions.

Main Results:

  • AT and TPS pathways both utilize outer membrane porins (AT translocator domains and TpsB proteins) that insert as beta-barrels.
  • Translocation in both pathways is folding-sensitive, with proteins crossing membranes in non-native conformations and folding at the cell surface.
  • AT pathways ensure specificity via a covalent link between passenger and translocator domains.
  • TPS pathways achieve specificity through a conserved N-proximal TPS domain on the secreted protein (TpsA) that interacts with its transporter (TpsB).

Conclusions:

  • The AT and TPS pathways represent distinct yet functionally related strategies for large protein secretion in Gram-negative bacteria.
  • The structural basis for specificity differs significantly, with AT relying on direct linkage and TPS on specific protein-protein interactions mediated by the TPS domain.
  • Understanding these pathways provides insights into bacterial virulence and potential therapeutic targets.