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Videos de Conceptos Relacionados

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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Published on: November 12, 2012

Los complejos de proteínas están bajo selección evolutiva para ensamblarse a través de vías ordenadas.

Joseph A Marsh1, Helena Hernández, Zoe Hall

  • 1EMBL-European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK.

Cell
|April 16, 2013
PubMed
Resumen
Este resumen es generado por máquina.

El orden de ensamblaje de las proteínas es crucial para la función biológica. El análisis evolutivo revela la selección de vías de ensamblaje conservadas, lo que demuestra su importancia fundamental en la formación de complejos proteicos.

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Área de la Ciencia:

  • La proteómica es la proteómica.
  • Biología evolutiva Biología evolutiva.
  • Biología Estructural Biología estructural.

Sus antecedentes:

  • Los complejos proteicos son esenciales para los procesos celulares.
  • Se supone que el orden secuencial del ensamblaje de proteínas en complejos es biológicamente significativo.
  • Comprender las vías de ensamblaje es clave para descifrar la función de las proteínas.

Objetivo del estudio:

  • Investigar la evidencia evolutiva para la selección en el ensamblaje ordenado de complejos proteicos.
  • Para determinar si las vías de ensamblaje de proteínas se pueden predecir a partir de la información estructural.
  • Explorar cómo los eventos de fusión génica impactan el ensamblaje y la evolución del complejo proteico.

Principales métodos:

  • Caracterización experimental de las vías de ensamblaje complejo heteromérico.
  • Predicción de las vías de ensamblaje a partir de estructuras tridimensionales de proteínas.
  • Mapeo de eventos de fusión génica de genomas secuenciados en vías de ensamblaje.
  • Análisis de datos de interacción estructurales y de alto rendimiento.

Principales resultados:

  • Las vías de ensamblaje de proteínas para complejos heteroméricos se pueden predecir a partir de sus estructuras.
  • La selección evolutiva favorece la conservación de órdenes específicos de ensamblaje de proteínas.
  • Los eventos de fusión génica tienden a simplificar las topologías complejas de proteínas, optimizando el ensamblaje.
  • Las restricciones estructurales de las proteínas influyen en el impacto de la fusión génica en el orden de ensamblaje.

Conclusiones:

  • Las vías ordenadas de ensamblaje de proteínas son biológicamente importantes y están sujetas a la selección evolutiva.
  • La estructura de las proteínas y los mecanismos evolutivos están íntimamente relacionados con el ensamblaje del complejo de proteínas.
  • Este estudio proporciona evidencia de todo el genoma para la importancia del ensamblaje ordenado en complejos proteicos.