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The Sec system.

A J Driessen1, P Fekkes, J P van der Wolk

  • 1Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands. a.j.m.driessen@biol.rug.nl

Current Opinion in Microbiology
|March 6, 1999
PubMed
Summary

SecB chaperone and translocase enzyme facilitate protein secretion in Escherichia coli. Protein translocation involves stepwise movements driven by conformational changes in the SecA motor protein.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Proteins destined for secretion in Escherichia coli possess an amino-terminal signal peptide.
  • Nascent protein chains associate with the export-specific chaperone SecB.
  • Protein translocation relies on the multisubunit membrane-bound enzyme complex known as translocase.

Purpose of the Study:

  • To elucidate the cascade of preprotein targeting events.
  • To understand the enzymatic mechanism of preprotein translocation.
  • To gain new insights into protein secretion pathways in E. coli.

Main Methods:

  • Analysis of protein synthesis and association with chaperones.
  • Characterization of the translocase complex components (SecA, SecY, SecE, SecG, SecD, SecF).
  • Investigation of preprotein translocation mechanisms, including nucleotide-induced conformational changes.

Main Results:

  • Identified the components of the translocase system, including SecA, SecYEG, and SecDF.
  • Demonstrated that preproteins are translocated in a stepwise manner.
  • Revealed that large nucleotide-induced conformational changes in SecA drive the translocation process.

Conclusions:

  • The SecB chaperone and translocase enzyme are crucial for bacterial protein secretion.
  • SecA acts as a molecular motor, utilizing conformational changes to propel preproteins across the membrane.
  • Understanding these mechanisms provides fundamental insights into protein export in prokaryotes.

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