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Detergent Purification of Membrane Proteins01:18

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Detergents are used to purify the integral proteins of the membrane. The hydrophobic portion of the detergent can replace membrane phospholipids while solubilizing the membrane proteins. When detergent monomers reach a specific concentration in a solution called critical micelle concentration (CMC), they form micelles. Above CMC, the concentration of the detergent monomers remains in equilibrium with the micelle. The number of detergent monomers present in the CMC varies for each detergent, and...
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Overview of Secretory Vesicles01:33

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

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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...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

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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.
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Export of Misfolded Proteins out of the ER01:32

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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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.
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Expression, Detergent Solubilization, and Purification of a Membrane Transporter, the MexB Multidrug Resistance Protein
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Estructura y función de un componente de membrana SecDF que mejora la exportación de proteínas.

Tomoya Tsukazaki1, Hiroyuki Mori, Yuka Echizen

  • 1Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Bunkyo-ku, Tokyo 113-0032, Japan.

Nature
|May 13, 2011
PubMed
Resumen

SecDF actúa como un chaperón de membrana, utilizando la fuerza motriz de protones para impulsar la translocación de proteínas independientes del ATP a través de las membranas bacterianas. Este complejo proteico facilita el transporte de proteínas y la biogénesis de proteínas de membrana.

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Área de la Ciencia:

  • Secreción de proteínas bacterianas secreción de proteínas bacterianas.
  • La biogénesis de las proteínas de membrana es la biogénesis de las proteínas de membrana.
  • Los mecanismos moleculares del transporte

Sus antecedentes:

  • La translocación de proteínas a través de las membranas bacterianas implica la translocación SecYEG y la ATPasa SecA.
  • La fuerza motriz de los protones y el complejo SecDF integrado en la membrana mejoran este proceso.
  • La función precisa de SecDF en la translocación y la biogénesis de proteínas de membrana sigue siendo incompletamente entendida.

Objetivo del estudio:

  • Aclarar las funciones estructurales y funcionales del complejo SecDF en la translocación de proteínas bacterianas.
  • Investigar el mecanismo por el cual el SecDF facilita el transporte de proteínas.
  • Determinar la contribución de la fuerza motriz del protón a la translocación mediada por SecDF.

Principales métodos:

  • Se ha determinado la estructura cristalina de Thermus thermophilus SecDF con una resolución de 3,3 Å.
  • Se realizó un análisis de mayor resolución de los dominios periplásmicos (P1 y P4) de SecDF.
  • Se realizaron ensayos de translocación in vitro y análisis electrofisiológicos de SecDF.

Principales resultados:

  • La estructura cristalina reveló un dominio transmembrana pseudo-simétrico (superfamilia RND) y los dominios periplásmicos P1 y P4.
  • El dominio periplasmático P1 sufre cambios conformacionales al unirse a la proteína desplegada.
  • SecDF facilita un paso de translocación independiente de ATP que requiere fuerza motriz de protones y exhibe conductividad de protones dependiente del pH y la presencia de sustrato.
  • Los residuos conservados en la interfaz transmembrana son cruciales para el movimiento de protones y preproteínas.

Conclusiones:

  • SecDF funciona como un chaperón integrado en la membrana.
  • La fuerza motriz de los protones impulsa un mecanismo de translocación de proteínas independiente del ATP mediado por SecDF.
  • SecDF juega un papel crítico en la facilitación del transporte de proteínas y potencialmente la biogénesis de proteínas de membrana a través de la conducción de protones y la flexibilidad conformacional.