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Conservation of Protein Domains Over Different Proteins02:26

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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Aggregation is a Context-Dependent Constraint on Protein Evolution.

Michele Monti1,2, Alexandros Armaos1,2, Marco Fantini3

  • 1Centre for Genomic Regulation (CRG), The Barcelona Institute for Science and Technology, Barcelona, Spain.

Frontiers in Molecular Biosciences
|July 5, 2021
PubMed
Summary
This summary is machine-generated.

Protein aggregation impacts molecular evolution differently depending on cellular context. Aggregation benefits human TAR DNA binding protein 43 (TDP-43) function but harms TEM-1 beta-lactamase activity, showing context-dependent evolutionary constraints.

Keywords:
cellular fitnesscomputational modeldeep scanningevolutionprotein aggregation

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biochemistry

Background:

  • Protein solubility is crucial for cellular functions; loss of solubility and aggregation can impair protein activity.
  • Understanding the link between protein evolution and aggregation is vital for comprehending molecular evolution.
  • Deep mutational scanning provides a powerful approach to study the effects of mutations on protein function and evolution.

Purpose of the Study:

  • To investigate the role of protein aggregation in molecular evolution using two distinct experimental systems.
  • To determine how cellular context influences the impact of protein aggregation on fitness.
  • To explore aggregation as a context-dependent constraint in molecular evolution.

Main Methods:

  • Analysis of two deep mutational scanning datasets: human TAR DNA binding protein 43 (TDP-43) in S. cerevisiae and TEM-1 beta-lactamase in E. coli.
  • Expression of protein mutants in their respective cellular hosts under selective pressures.
  • Assessment of the relationship between protein aggregation and host cell fitness.

Main Results:

  • Protein aggregation has differential effects on cell fitness depending on the protein and cellular environment.
  • For TDP-43, aggregation is associated with increased cell fitness, potentially by preventing aberrant interactions.
  • For TEM-1 beta-lactamase, aggregation is linked to decreased cell fitness due to functional inactivation.

Conclusions:

  • Protein aggregation is a significant context-dependent constraint in molecular evolution.
  • The impact of aggregation on fitness varies across different proteins and cellular systems.
  • This study opens new avenues for researching the role of protein aggregation in cellular processes and evolution.