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The dynamic properties of a nuclear coactivator binding domain are evolutionarily conserved
Elin Karlsson1, Frieda A Sorgenfrei1,2, Eva Andersson1
1Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, SE-75123, Uppsala, Sweden.
Communications Biology
|March 31, 2022
Summary
Intrinsically disordered proteins like NCBD evolve dynamically. Ancient and human NCBD show maintained flexibility, suggesting purifying selection preserves these crucial protein dynamics for function.
Area of Science:
- Biochemistry
- Evolutionary Biology
- Structural Biology
Background:
- Protein evolution is shaped by structure-function constraints.
- Intrinsically disordered proteins (IDPs) offer evolutionary plasticity.
- Limited data exists on the molecular mechanisms of IDP evolution.
Purpose of the Study:
- To investigate the evolutionary trajectory of the Nuclear Coactivator Binding Domain (NCBD).
- To compare the structure and dynamics of ancient and human NCBD.
- To understand the role of protein dynamics in the evolution of intrinsically disordered proteins.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy.
- Circular dichroism (CD) spectroscopy.
- Kinetic assays.
Main Results:
- Ancient and human NCBD exhibit similar dynamic, ligand-free biophysical properties.
- NCBD has increased thermodynamic stability over evolutionary time.
- The molten-globule-like nature and dynamics of NCBD are conserved.
Conclusions:
- The dynamic properties of NCBD are likely maintained by purifying selection.
- Conserved dynamics are essential for NCBD's function in mediating protein-protein interactions.
- NCBD serves as a model for studying the evolution of intrinsically disordered proteins.
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