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Related Concept Videos

Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

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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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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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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.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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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.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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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
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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Gram-negative Bacterial Protein Secretion Systems01:17

Gram-negative Bacterial Protein Secretion Systems

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Gram-negative bacteria utilize sophisticated protein secretion systems to transport proteins across their double-membrane envelope into the extracellular environment or host cells. Based on their mechanism of action, these systems are classified into one-step and two-step pathways.One-Step Secretion Systems (Types I, III, IV, and VI)One-step secretion systems bypass the periplasm entirely, forming a continuous channel that spans both the inner and outer membranes:Type I Secretion System (T1SS):...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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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.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
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Related Experiment Video

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Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
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Protein export through the bacterial Sec pathway.

Alexandra Tsirigotaki1, Jozefien De Geyter1, Nikolina Šoštaric1

  • 1Laboratory of Molecular Bacteriology, Department of Microbiology and Immunology, Rega Institute for Medical Research, Katholieke Universiteit Leuven (KU Leuven), B-3000 Leuven, Belgium.

Nature Reviews. Microbiology
|November 29, 2016
PubMed
Summary
This summary is machine-generated.

The general secretory (Sec) pathway machinery exports proteins across bacterial membranes. Recent studies reveal how protein targeting, translocation, and release are regulated by the SecYEG channel and SecA motor.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • The general secretory (Sec) pathway is crucial for exporting proteins across the plasma membrane in bacteria.
  • Proteins destined for secretion are synthesized as pre-proteins with signal peptides that guide them to the export machinery.
  • Chaperones and conformational signals play key roles in targeting pre-proteins to the SecYEG channel.

Purpose of the Study:

  • To review recent biochemical, structural, and mechanistic insights into the bacterial Sec pathway.
  • To elucidate the regulation and dynamics of the SecYEG channel and its ATPase motor, SecA.
  • To present models for the mechanisms and energetics of Sec-dependent protein secretion.

Main Methods:

  • Review of recent biochemical and structural studies.
  • Analysis of mechanistic insights into protein targeting and translocation.
  • Integration of data on the SecYEG channel, SecA motor, and pre-protein interactions.

Main Results:

  • Advances in understanding chaperone interactions and conformational checkpoints in pre-protein targeting.
  • New structural and mechanistic details of the SecYEG channel and SecA ATPase motor.
  • Elucidation of allosteric crosstalk mediating protein secretion.

Conclusions:

  • The Sec pathway involves intricate regulation of sorting, targeting, translocation, and release steps.
  • Co-translational and post-translational export modes are governed by the dynamic interplay of the SecYEG channel, SecA, ribosomes, and pre-proteins.
  • Conceptual models provide insights into the mechanisms and energetics of bacterial protein secretion.