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Cells use energy-requiring bulk transport mechanisms to transfer large particles, or large amounts of small particles, into or out of the cell. The cells envelop the particles in spherical membranes called vesicles or vacuoles. Vesicles that transport material into the cell are built from the cell membrane. These vesicles encapsulate external molecules and transport them into the cell in a process called endocytosis.
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Protein Transport into the Inner Mitochondrial Membrane01:34

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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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Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
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Protein Transport to the Outer Chloroplast Membrane01:11

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Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
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Protein Import into the Peroxisomes01:27

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Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
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Protein Transport to the Inner Chloroplast Membrane01:18

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Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
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Acompañantes moleculares en el plegamiento de proteínas celulares.

F U Hartl1

  • 1Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York 10021, USA.

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|June 13, 1996
PubMed
Resumen

Las chaperonas moleculares son proteínas esenciales que evitan estructuras de proteínas mal plegadas en las células. Las familias Hsp70 y chaperonina utilizan mecanismos dependientes del ATP para ayudar en el plegamiento de las proteínas, especialmente bajo estrés.

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Área de la Ciencia:

  • Biología celular Biología celular.
  • La bioquímica es la bioquímica.
  • El plegamiento de las proteínas.

Sus antecedentes:

  • Las proteínas recién sintetizadas requieren asistencia para el plegamiento adecuado dentro de la célula.
  • Las chaperonas moleculares son proteínas conservadas cruciales para prevenir el plegamiento incorrecto de las proteínas.
  • El estrés celular, como el choque térmico, aumenta el riesgo de mal plegamiento de las proteínas.

Objetivo del estudio:

  • Para resumir la comprensión de los mecanismos de acompañamiento molecular en el plegamiento de las proteínas.
  • Para resaltar los roles de las familias Hsp70 y chaperoninas.
  • Describir la función cooperativa de las chaperonas para ayudar a nuevas cadenas polipeptídicas.

Principales métodos:

  • Revisión de la literatura existente sobre las chaperonas moleculares.
  • Análisis de los mecanismos dependientes del ATP.
  • Examen de la cooperación de los chaperones en el plegamiento de las proteínas.

Principales resultados:

  • Las chaperonas moleculares evitan estructuras de proteínas mal plegadas bajo condiciones normales y de estrés.
  • Las familias Hsp70 y chaperonina utilizan mecanismos dependientes del ATP para el plegamiento de las proteínas.
  • Estas familias de acompañantes pueden cooperar para facilitar el plegamiento de nuevas cadenas de polipéptidos.

Conclusiones:

  • Los acompañantes moleculares son vitales para mantener la proteostasis.
  • Los mecanismos dependientes del ATP son fundamentales para la función de la chaperona.
  • La acción cooperativa de las chaperonas mejora su eficiencia en el plegamiento de las proteínas.