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Related Concept Videos

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
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Translocation of Proteins into the Mitochondria01:19

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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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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Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

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Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
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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
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Bidirectional Peptide Translocation through Ultrasmall Solid-State Nanopores.

Guanghao Wei1, Rui Hu1, Wenlong Lu1

  • 1State Key Lab for Mesoscopic Physics and Frontiers Science Center for Nano-optoelectronics School of Physics, Peking University, Beijing 100871, China.

Langmuir : the ACS Journal of Surfaces and Colloids
|September 20, 2024
PubMed
Summary
This summary is machine-generated.

Researchers used ultrasmall solid-state nanopores to detect single peptide chains. This novel method revealed unique bidirectional translocation signals, paving the way for high-resolution peptide detection and fingerprinting.

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Area of Science:

  • Biophysics
  • Analytical Chemistry
  • Biochemistry

Background:

  • Understanding polypeptide configuration and amino acid sequences is crucial for life processes and biological applications.
  • Single-molecule detection technologies, like nanopores, offer advantages for real-time dynamics analysis.

Purpose of the Study:

  • To design and utilize a novel peptide chain for ultrasmall solid-state nanopore detection.
  • To investigate the translocation behavior of peptides within nanopores and confirm findings with natural peptides.

Main Methods:

  • Design of a specialized peptide chain with 10 arginine residues.
  • Single-molecule detection using ultrasmall solid-state nanopores (2-3 nm).
  • Analysis of bidirectional translocation signals based on charge distribution and nanopore interactions.

Main Results:

  • Successful single-molecule detection of the designed peptide chain.
  • Observation and explanation of unique bidirectional translocation signals.
  • Validation of the approach using natural peptides (histatin-5 and angiopep-2).

Conclusions:

  • Ultrasmall solid-state nanopores can effectively detect single peptide chains.
  • Peptide charge distribution and nanopore interactions dictate translocation behavior.
  • The developed method enables multiple detections of the same peptide, offering potential for high-resolution peptide fingerprinting.