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Overview of Protein Sorting and Transport01:45

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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
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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 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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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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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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Translocation, Rejection and Trapping of Polyampholytes.

Yeong-Beom Kim1, Min-Kyung Chae1, Jeong-Man Park2

  • 1Department of Physics and Astronomy, Sejong University, Seoul 05006, Korea.

Polymers
|February 26, 2022
PubMed
Summary

This study reveals that polymer translocation through pores depends heavily on sequence, with early stages influenced by the leading charge and later stages by trapped states. This offers insights into protein behavior, particularly intrinsically disordered proteins (IDPs).

Keywords:
Monte Carlo simulationdrift-diffusionpolyampholytesprobability distribution functiontranslocation

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Area of Science:

  • Polymer Physics
  • Computational Biophysics
  • Statistical Mechanics of Disordered Systems

Background:

  • Polyampholytes (PAs) are polymers with both positive and negative monomers, analogous to proteins.
  • Unlike proteins with defined sequences, synthetic PAs have random charge sequences.
  • Understanding PA translocation through pores is crucial for biological processes and synthetic polymer behavior.

Purpose of the Study:

  • To investigate the translocation behavior of random polyampholyte chains through a pore under an electric field.
  • To analyze the influence of sequence-specific charge distribution on translocation dynamics.
  • To provide theoretical insights and operational criteria for predicting PA translocation.

Main Methods:

  • Monte Carlo simulations of polyampholyte chains translocating through an extended asymmetric pore.
  • Incorporation of a realistic translocation potential profile.
  • Analysis of translocation (translocation vs. rejection) for various sequences and chain lengths (N=20 and N=40).

Main Results:

  • Early translocation/rejection is sequence-dependent on the leading charges, while late stages are governed by escaping trapped states.
  • Translocation time distributions exhibit power-law tails, indicating a population of slowly relaxing trapped sequences.
  • Favorable net charge enhances power-law decay, and translocation is highly sequence-selective, even for highly charged chains.

Conclusions:

  • Translocation dynamics are critically dependent on the specific charge sequence and the presence of antagonistic barriers.
  • Findings provide a framework for understanding the translocation of intrinsically disordered proteins (IDPs) as PAs.
  • Operational criteria are established for predicting sequence-specific translocation behavior.