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High affinity between CREBBP/p300 and NCOA evolved in vertebrates.

Elin Karlsson1, Amanda Lindberg1, Eva Andersson1

  • 1Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden.

Protein Science : a Publication of the Protein Society
|April 25, 2020
PubMed
Summary

The high-affinity interaction between CREBBP/p300 and NCOA protein domains evolved in vertebrates, not all deuterostomes. This finding impacts understanding of transcriptional regulation evolution.

Keywords:
ACTRCBPCIDCREBBPNCBDechinodermintrinsically disordered proteinp300protein evolutionprotein-protein interaction

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Area of Science:

  • Evolutionary biology
  • Molecular biology
  • Genetics

Background:

  • The interaction between transcriptional coactivators CREBBP/p300 and NCOA is crucial for gene regulation.
  • This interaction is mediated by intrinsically disordered domains: NCBD (from CREBBP/p300) and CID (from NCOA).
  • The CID domain appeared in deuterostomes, but the evolution of high-affinity interaction within this clade is unclear.

Purpose of the Study:

  • To investigate the evolutionary timeline of the high-affinity NCBD:CID interaction within deuterostomes.
  • To determine if all extant deuterostome species possess this high-affinity interaction.

Main Methods:

  • Expression and affinity measurement of NCBD and CID domains from various deuterostome species.
  • Comparative analysis of interaction affinities across different evolutionary branches.

Main Results:

  • All examined vertebrate species exhibit high-affinity NCBD:CID interactions.
  • The interaction in the purple sea urchin (an echinoderm) shows similar affinity to proposed ancestral domains.
  • This suggests the high-affinity interaction likely evolved specifically within the vertebrate lineage.

Conclusions:

  • The high-affinity interaction between CREBBP/p300 and NCOA appears to have evolved in vertebrates.
  • The essentiality of this interaction in non-vertebrate deuterostomes is questioned.
  • Provides an example of transcriptional regulation evolution via protein-domain innovations.