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Related Concept Videos

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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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.
Sec61 protein conducting channel
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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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Post-translational Translocation of Proteins to the RER01:27

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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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Insertion of Single-pass Transmembrane Proteins in the RER01:26

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Bacterial Translocation and Protein Secretion01:26

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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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The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
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Crystal structures of a polypeptide processing and secretion transporter.

David Yin-wei Lin1, Shuo Huang2, Jue Chen1

  • 11] Laboratory of Membrane Biology and Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA [2] Howard Hughes Medical Institute, 1230 York Avenue, New York, New York 10065, USA.

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Summary
This summary is machine-generated.

Peptidase-containing ATP-binding cassette transporters (PCATs) are simple bacterial protein secretion machines. Crystal structures reveal how ATP binding regulates PCATs

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Area of Science:

  • Microbiology and Molecular Biology
  • Protein Secretion Mechanisms
  • Bacterial Cell Biology

Background:

  • Bacteria utilize secreted peptides and proteins for communication, competition, and host manipulation.
  • Protein translocation across bacterial membranes involves diverse machineries.
  • Peptidase-containing ATP-binding cassette transporters (PCATs) represent a structurally simple class of these systems.

Purpose of the Study:

  • To elucidate the structural and functional mechanisms of PCATs in protein translocation.
  • To investigate the role of ATP binding in regulating PCAT activity and substrate processing.

Main Methods:

  • X-ray crystallography of PCAT1 from Clostridium thermocellum in distinct conformations.
  • Biochemical assays to assess protease activity and translocation pathway function.

Main Results:

  • Determined crystal structures of PCAT1 revealing a large α-helical barrel translocation pathway.
  • Demonstrated that the pathway can accommodate small folded proteins.
  • Showed ATP binding dynamically controls pathway access and protease activity, coupling substrate processing to export.

Conclusions:

  • PCATs employ an ATP-dependent mechanism to coordinate substrate maturation and translocation.
  • The elucidated mechanism provides insights into bacterial protein secretion and potential therapeutic targets.