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Porin Insertion in the Outer Mitochondrial Membrane01:12

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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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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.
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Protein Translocation Machinery on the ER Membrane01:28

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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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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Bacterial Translocation and Protein Secretion01:26

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Video Experimental Relacionado

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Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
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Bases estructurales de la inserción de proteínas de la membrana externa por el complejo BAM

Yinghong Gu1, Huanyu Li1, Haohao Dong1

  • 1Biomedical Research Centre, Norwich Medical School, University of East Anglia, Norwich Research Park, Norwich NR4 7TJ, UK.

Nature
|February 23, 2016
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Resumen

El mecanismo de ensamblaje de proteínas de la membrana externa bacteriana (BAM) ahora es más claro. Los estudios estructurales revelan cómo BamA y las proteínas asociadas giran para insertar nuevas proteínas de la membrana externa (OMPs) en la envoltura celular.

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Área de la Ciencia:

  • Biología estructural
  • Biología molecular
  • La bioquímica

Sus antecedentes:

  • Las proteínas de la membrana externa (OMP) son cruciales para las bacterias gramnegativas, las mitocondrias y los cloroplastos.
  • El complejo de maquinaria de ensamblaje de barril β (BAM) facilita la inserción y el plegamiento de la OMP en la membrana externa.
  • El mecanismo preciso de la biogénesis de la OMP mediada por BAM sigue siendo en gran medida desconocido debido a la falta de datos estructurales.

Objetivo del estudio:

  • Para aclarar el mecanismo de inserción de proteínas de la membrana externa por el complejo BAM.
  • Proporcionar información estructural de alta resolución sobre el complejo BAM de Escherichia coli.
  • Comprender las interacciones dinámicas entre las subunidades de BAM durante la biogénesis de OMP.

Principales métodos:

  • Cristalografía de rayos X para determinar la estructura del complejo BAM en diferentes estados.
  • Ensayos bioquímicos para estudiar la función de los componentes del complejo BAM.
  • Simulaciones de dinámica molecular para analizar los movimientos dinámicos dentro del complejo BAM.

Principales resultados:

  • Se determinaron dos estructuras cristalinas distintas del complejo BAM de Escherichia coli: un estado abierto hacia adentro y un estado abierto lateral.
  • Las estructuras revelan una arquitectura de anillo formada por los cinco dominios asociados al transporte de polipéptidos de BamA, asociados con cuatro lipoproteínas (BamB-BamE).
  • Los datos estructurales y funcionales indican que la rotación de las lipoproteínas asociadas con respecto al barril β de BamA impulsa la inserción de PMO nacientes.

Conclusiones:

  • El estudio proporciona instantáneas estructurales sin precedentes del complejo BAM, revelando su naturaleza dinámica.
  • Los hallazgos aclaran un mecanismo basado en la rotación para la inserción de OMP mediada por el complejo BAM.
  • Este trabajo avanza significativamente nuestra comprensión de un proceso fundamental en la biogénesis de las proteínas esenciales de la membrana.