Deamidation alters interactions of β-crystallins in hetero-oligomers
2008
How Deamidation Affects Protein Interactions in the Eye Lens
publication
Evidence: moderate
Author Information
Author(s): Takata Takumi, Woodbury Luke G., Lampi Kirsten J.
Primary Institution: Oregon Health & Science University
Hypothesis
Does deamidation alter the interaction of βA3 with other β-crystallin subunits?
Conclusion
Deamidation decreased formation of hetero-oligomers between β-crystallin subunits, which may contribute to cataract formation.
Supporting Evidence
- Deamidation at the interface in the βA3 dimer decreased the formation of hetero-oligomers with βB1 and βB2.
- βB1 was able to prevent precipitation of deamidated βA3 during thermal denaturation.
- An excess accumulation of deamidated β-crystallins may disrupt normal protein interactions in the lens.
Takeaway
When proteins in the eye lens get older, they change in a way that makes them stick together less, which can lead to cataracts.
Methodology
The study used site-directed mutagenesis to mimic deamidation and analyzed protein interactions through size exclusion chromatography and fluorescence spectroscopy.
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