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RAD23B acquires a copper metalloadaptor function in amphibian-to-reptile evolution to increase metabolism and

Tong Xiao1, Dan He2, Danqian Liu3

  • 1Department of Chemistry, Princeton University, Princeton, NJ, USA; Department of Chemistry, University of California, Berkeley, Berkeley, CA, USA.

Molecular Cell
|September 19, 2025
PubMed
Summary

The DNA repair protein RAD23B evolved a new function in reptiles, binding copper to regulate metabolism and DNA repair. This adaptation helps manage toxic copper levels and supports energy needs in vital cells.

Keywords:
Amniota evolutionCTR1/SLC31A1Rad23bmetalloadaptormetalloallosterymitochondrial metabolismsleep and wake behaviortransition metal signaling

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Area of Science:

  • Evolutionary biology
  • Molecular biology
  • Biochemistry

Background:

  • Increasing brain complexity is a hallmark of species evolution.
  • The DNA repair protein RAD23B plays a role in maintaining genomic integrity.

Purpose of the Study:

  • To investigate the evolutionary changes in RAD23B function during the transition from amphibians to reptiles.
  • To understand how RAD23B integrates metabolism and DNA repair through nutrient regulation.

Main Methods:

  • Comparative genomics and proteomics analysis.
  • Biochemical assays to determine protein function and copper binding.
  • Cellular and physiological studies in model organisms.

Main Results:

  • RAD23B acquired a metalloadaptor function, gaining a copper-binding site (H274/H323).
  • This site facilitates copper transfer from CTR1 to metallochaperones, making DNA repair copper-dependent.
  • This regulation allows tolerance of toxic copper and supports high-energy demands.

Conclusions:

  • RAD23B's evolution represents a key adaptation for increased brain complexity and metabolic regulation.
  • The dual role of RAD23B in copper metabolism and DNA repair is crucial for cellular function in physiology and disease.
  • This mechanism is relevant to neurons and cancer cells with high energetic requirements.