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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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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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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...
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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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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
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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.
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Assembly of Signaling Complexes

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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.
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Updated: Sep 3, 2025

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions
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Large protein complex interfaces have evolved to promote cotranslational assembly.

Mihaly Badonyi1, Joseph A Marsh1

  • 1MRC Human Genetics Unit, Institute of Genetics and Cancer, University of Edinburgh, Edinburgh, United Kingdom.

Elife
|July 28, 2022
PubMed
Summary
This summary is machine-generated.

Protein complex assembly is efficient via cotranslational assembly. Large subunit interfaces evolved to promote this process, ensuring successful protein binding during translation.

Keywords:
E. coliS. cerevisiaecomputational biologycotranslational foldingevolutionary biologyhumanprotein interactionsribosome profilingstructural bioinformaticssystems biology

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Systems Biology

Background:

  • Efficient and precise protein complex assembly is crucial to prevent misfolding and unwanted interactions.
  • Cotranslational assembly, where subunits assemble during protein synthesis, is a proposed mechanism for enhancing assembly efficiency.
  • However, the specific properties of protein complexes that engage in cotranslational assembly remain largely unexplored.

Purpose of the Study:

  • To investigate the characteristics of protein complexes that undergo cotranslational assembly.
  • To determine if large intermolecular interfaces are a driving factor for cotranslational assembly.
  • To explore the evolutionary implications of interface size in facilitating cotranslational subunit binding.

Main Methods:

  • Analysis of proteome-specific protein complex structures.
  • Integration with publicly available ribosome profiling data.
  • Comparative analysis of N-terminal and C-terminal interface sizes in heteromeric subunits across different species (bacteria, yeast, human).

Main Results:

  • Cotranslational assembly is prevalent in protein complexes with large intermolecular interfaces.
  • The N-terminal interface is larger than the C-terminal interface in a majority of heteromeric subunits (54%).
  • This size difference is more pronounced (64%) when excluding subunits with small interfaces, suggesting an evolutionary adaptation for cotranslational binding.

Conclusions:

  • Large intermolecular interfaces have likely evolved to promote efficient cotranslational assembly.
  • This evolutionary adaptation maximizes the probability of successful subunit binding during protein synthesis.
  • Cotranslational assembly is a key strategy for ensuring the fidelity and efficiency of protein complex formation.