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Related Concept Videos

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-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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Related Experiment Video

Updated: May 10, 2026

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
14:58

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

Protein complexes are under evolutionary selection to assemble via ordered pathways.

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
Summary
This summary is machine-generated.

Protein assembly order is crucial for biological function. Evolutionary analysis reveals selection for conserved assembly pathways, demonstrating their fundamental importance in protein complex formation.

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Area of Science:

  • Proteomics
  • Evolutionary Biology
  • Structural Biology

Background:

  • Protein complexes are essential for cellular processes.
  • The sequential order of protein assembly into complexes is hypothesized to be biologically significant.
  • Understanding assembly pathways is key to deciphering protein function.

Purpose of the Study:

  • To investigate evolutionary evidence for selection on ordered protein complex assembly.
  • To determine if protein assembly pathways can be predicted from structural information.
  • To explore how gene fusion events impact protein complex assembly and evolution.

Main Methods:

  • Experimental characterization of heteromeric complex assembly pathways.
  • Prediction of assembly pathways from three-dimensional protein structures.
  • Mapping gene fusion events from sequenced genomes onto assembly pathways.
  • Analysis of structural and high-throughput interaction data.

Main Results:

  • Protein assembly pathways for heteromeric complexes can be predicted from their structures.
  • Evolutionary selection favors the conservation of specific protein assembly orders.
  • Gene fusion events tend to simplify protein complex topologies, optimizing assembly.
  • Protein structural constraints influence the impact of gene fusion on assembly order.

Conclusions:

  • Ordered protein assembly pathways are biologically important and subject to evolutionary selection.
  • Protein structure and evolutionary mechanisms are intimately linked to protein complex assembly.
  • This study provides genome-wide evidence for the significance of ordered assembly in protein complexes.