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Related Concept Videos

Nuclear Export01:42

Nuclear Export

The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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...
Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

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...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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...
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

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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Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

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Published on: August 10, 2021

Emerging themes in SecA2-mediated protein export.

Meghan E Feltcher1, Miriam Braunstein

  • 1Department of Microbiology and Immunology, School of Medicine, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-27290, USA.

Nature Reviews. Microbiology
|September 25, 2012
PubMed
Summary

Bacteria use the general secretion (Sec) pathway for protein export, powered by SecA ATPase. This review focuses on the less-understood SecA2 system, exploring its diverse functions and future research directions.

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Area of Science:

  • Bacteriology
  • Molecular Biology
  • Protein Secretion

Background:

  • The general secretion (Sec) pathway is crucial for bacterial protein export.
  • SecA ATPase powers the Sec pathway.
  • Some bacteria, like mycobacteria, have two SecA proteins: SecA1 and SecA2.

Purpose of the Study:

  • To review the current understanding of SecA2 systems.
  • To outline future research directions for SecA2 function.

Main Methods:

  • Literature review of SecA2 systems.
  • Analysis of SecA2 substrate specificity.
  • Exploration of SecA2's role in virulence.

Main Results:

  • SecA1 exports most bacterial proteins.
  • SecA2 exports a specific subset of substrates.
  • SecA2 is implicated in bacterial virulence.

Conclusions:

  • SecA2 function is less understood than SecA1.
  • Further research is needed to elucidate SecA2's diverse roles and systems.