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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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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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Next-generation sequencing technologies have created large genomic databases of a variety of animals and plants. Ever since the human genome project was completed, scientists studied the genome of primates, mammals, and other phylogenetically distant living beings. Such large-scale  studies have provided new insights into the evolutionary relationship between 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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The genomes of eukaryotes are punctuated by long stretches of sequence which do not code for proteins or RNAs. Although some of these regions do contain crucial regulatory sequences, the vast majority of this DNA serves no known function. Typically, these regions of the genome are the ones in which the fastest change, in evolutionary terms, is observed, because there is typically little to no selection pressure acting on these regions to preserve their sequences.
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Updated: Aug 27, 2025

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation
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Correlation between protein abundance and sequence conservation: what do recent experiments say?

Camille Bédard1, Angel F Cisneros2, David Jordan2

  • 1Département de Biologie, Faculté des Sciences et de Génie, Université Laval, G1V 0A6, Canada; Institut de Biologie Intégrative et des Systèmes, Université Laval, G1V 0A6, Canada; PROTEO, Le regroupement québécois de recherche sur la fonction, l'ingénierie et les applications des protéines, Université Laval, G1V 0A6, Canada; Centre de Recherche sur les Données Massives, Université Laval, G1V 0A6, Canada.

Current Opinion in Genetics & Development
|September 26, 2022
PubMed
Summary
This summary is machine-generated.

Highly expressed proteins evolve slower than lowly expressed ones due to physical and chemical constraints within cells. This review explores hypotheses and experiments explaining this protein evolution rate and abundance correlation.

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Biophysics

Background:

  • Cellular parameters are constrained by physical and chemical forces.
  • A key constraint is the negative correlation between protein evolution rate and cellular abundance.
  • Highly expressed proteins exhibit slower evolution compared to lowly expressed proteins.

Purpose of the Study:

  • To review hypotheses explaining the slower evolution of highly expressed proteins.
  • To examine experimental evidence supporting these hypotheses.
  • To discuss recent experiments testing these predictions.

Main Methods:

  • Literature review of hypotheses (e.g., mRNA stability, misfolding, misinteraction avoidance).
  • Analysis of existing experimental data supporting or refuting hypotheses.
  • Discussion of recent experimental designs and findings.

Main Results:

  • Several hypotheses exist, including mRNA stability, misfolding avoidance, and misinteraction avoidance.
  • Experimental evidence varies in its support for each hypothesis.
  • Recent experiments provide new insights into the mechanisms driving the observed correlation.

Conclusions:

  • The relationship between protein expression and evolution rate is complex and multifactorial.
  • Physical and chemical constraints significantly influence protein evolution.
  • Further experimental validation is crucial to fully elucidate the underlying mechanisms.