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BARD1 is an ATPase activating protein for OLA1
Ting Chen1, Hung-Wei Yeh1, Po-Pang Chen1
1Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 300044, Taiwan.
Biochimica Et Biophysica Acta. General Subjects
|February 8, 2022
Summary
The BARD1 protein activates OLA1 ATPase activity, crucial for centrosome duplication. A cancer-linked mutation in BARD1 impairs this activation, potentially causing centrosome abnormalities.
Area of Science:
- Molecular biology
- Biochemistry
- Structural biology
Background:
- OLA1 (Olap1) is a P-loop ATPase involved in centrosome duplication.
- Its interaction with BRCA1-associated BARD1 is critical, as disruption leads to centrosome amplification.
- The precise mechanism of the OLA1-BARD1 complex remains unclear.
Purpose of the Study:
- To elucidate the molecular basis of the OLA1-BARD1 interaction.
- To understand how BARD1 regulates OLA1 ATPase activity.
- To investigate the impact of a cancer-associated mutation on this interaction.
Main Methods:
- Biophysical analyses
- Biochemical assays
- Structural analyses (crystallography)
- Enzyme kinetics
Main Results:
- The BARD1 BRCT domain binds OLA1's TGS domain via the BUDR motif, enhancing OLA1's ATPase activity (kcat).
- This interaction is nucleotide-dependent.
- A cancer-related BARD1 mutation (V695L) reduces OLA1 activation by disrupting the binding site.
Conclusions:
- BARD1 acts as an allosteric ATPase activating protein for OLA1.
- The BARD1 BRCT domain controls OLA1 activity through a conserved motif.
- The V695L mutation highlights the clinical relevance of this regulatory mechanism in centrosome biology.
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