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Videos de Conceptos Relacionados

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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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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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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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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Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

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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.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
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Video Experimental Relacionado

Updated: Apr 6, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
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Estructuras cristalinas de un transportador de procesamiento y secreción de polipéptidos

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.

Nature
|July 24, 2015
PubMed
Resumen

Los transportadores de casete de unión de ATP (PCAT) que contienen peptidasa son máquinas simples de secreción de proteínas bacterianas. Las estructuras cristalinas revelan cómo la unión de ATP regula las PCAT

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Área de la Ciencia:

  • Microbiología y Biología Molecular
  • Mecanismos de secreción de proteínas
  • Biología celular bacteriana

Sus antecedentes:

  • Las bacterias utilizan péptidos y proteínas secretadas para la comunicación, la competencia y la manipulación del huésped.
  • La translocación de proteínas a través de las membranas bacterianas implica diversas maquinarias.
  • Los transportadores de unión de ATP (PCAT) que contienen peptidasa representan una clase estructuralmente simple de estos sistemas.

Objetivo del estudio:

  • Aclarar los mecanismos estructurales y funcionales de las PCAT en la translocación de proteínas.
  • Investigar el papel de la unión de ATP en la regulación de la actividad PCAT y el procesamiento del sustrato.

Principales métodos:

  • Cristalografía de rayos X de PCAT1 de Clostridium thermocellum en conformaciones distintas.
  • Ensayos bioquímicos para evaluar la actividad de la proteasa y la función de la vía de translocación.

Principales resultados:

  • Determinación de las estructuras cristalinas de PCAT1 que revelan una gran vía de translocación de barril α-helical.
  • Demostró que la vía puede acomodar pequeñas proteínas plegadas.
  • Se ha demostrado que la unión de ATP controla dinámicamente el acceso a la vía y la actividad de la proteasa, acoplando el procesamiento del sustrato a la exportación.

Conclusiones:

  • Los PCAT emplean un mecanismo dependiente del ATP para coordinar la maduración y la translocación del sustrato.
  • El mecanismo elucidado proporciona información sobre la secreción de proteínas bacterianas y posibles objetivos terapéuticos.