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Protein Complexes with Interchangeable Parts01:57

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Analyzing Large Protein Complexes by Structural Mass Spectrometry
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Structural and evolutionary versatility in protein complexes with uneven stoichiometry.

Joseph A Marsh1, Holly A Rees2, Sebastian E Ahnert3

  • 11] MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, UK [2] European Molecular Biology Laboratory, European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, UK.

Nature Communications
|March 17, 2015
PubMed
Summary
This summary is machine-generated.

Uneven protein stoichiometry, where protein complexes have differing numbers of subunits, is common. This structural feature, driven by subunit asymmetry, is enriched in bacteria due to their self-assembly tendencies.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Evolutionary Biology

Background:

  • Proteins assemble into complexes with diverse quaternary structures.
  • Most known heteromeric protein complexes exhibit even stoichiometry, with equal numbers of each subunit type.
  • A notable minority of complexes display uneven stoichiometry, featuring unequal subunit ratios.

Purpose of the Study:

  • To investigate the prevalence of uneven protein stoichiometry in vitro and in vivo.
  • To identify the structural mechanisms enabling uneven stoichiometry in protein complexes.
  • To analyze the evolutionary distribution of uneven stoichiometry, comparing bacterial and eukaryotic proteomes.

Main Methods:

  • Bioinformatic analysis of protein complex structures and stoichiometry.
  • Structural modeling to elucidate subunit interaction interfaces.
  • Comparative evolutionary analysis of protein assembly across different domains of life.

Main Results:

  • Uneven stoichiometry is prevalent in vitro and likely common in vivo.
  • Six distinct structural mechanisms facilitate uneven stoichiometry, often involving subunit asymmetry.
  • Uneven stoichiometry is significantly enriched in bacteria compared to eukaryotes.

Conclusions:

  • Bacterial proteins exhibit a greater propensity for self-assembly and homomeric interactions, even within heteromeric complexes.
  • This increased self-assembly tendency in bacteria contributes to the observed enrichment of uneven stoichiometry.
  • Understanding the structural basis and evolutionary drivers of uneven stoichiometry provides insights into protein complex assembly and function.