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Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
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ATP-binding cassette or ABC transporters are a class of ATP-driven pumps that hydrolyze ATP to move solutes across the membrane. They can be grouped into importers and exporters. While exporters are present in all domains of life, importers exist only in bacteria and some plants.
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ABC Transporters: Exporter01:31

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ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...
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Cotranslational Protein Translocation01:20

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
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Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles
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BamA is required for autotransporter secretion.

David Ryoo1, Marcella Orwick Rydmark2, Yui Tik Pang3

  • 1Interdisciplinary Bioengineering Graduate Program, Georgia Institute of Technology, Atlanta, GA 30332, United States of America.

Biochimica Et Biophysica Acta. General Subjects
|March 2, 2020
PubMed
Summary

Autotransporter secretion in Gram-negative bacteria likely involves the β-barrel assembly machinery (BAM) complex and an incomplete autotransporter β-barrel, not a fully formed barrel or hairpin intermediate.

Keywords:
AutotransportersMembrane proteinsMolecular dynamicsSecretion systems

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Structural Biology

Background:

  • Gram-negative bacteria utilize autotransporters to secrete virulence factors.
  • Autotransporter structure comprises a passenger domain and a β-barrel for export.
  • The β-barrel assembly machinery (BAM) complex is involved in β-barrel folding and insertion.

Purpose of the Study:

  • To investigate the mechanism of autotransporter passenger domain secretion.
  • To differentiate between the hairpin model and the BamA-assisted model of secretion.

Main Methods:

  • Molecular dynamics simulations were employed.
  • Simulations focused on autotransporters EspP and YadA.

Main Results:

  • Autotransporter β-barrels showed structural distortions when accommodating passenger domains in a hairpin.
  • Secretion through EspP's β-barrel required more force than through BamA.

Conclusions:

  • The hairpin model is unlikely due to structural constraints.
  • Autotransporter secretion likely involves BamA and a partially formed β-barrel.