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Single Droplet Digital Polymerase Chain Reaction for Comprehensive and Simultaneous Detection of Mutations in Hotspot Regions
Published on: September 25, 2018
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Single mutations in the ε subunit from thermophilic
Alexander Krah1,2, Peter J Bond3,4
1School of Computational Sciences, Korea Institute for Advanced Study, Seoul, Republic of Korea.
Peerj
|September 12, 2018
Summary
Bacterial ATP synthase ε subunits sense ATP levels. Single mutations R103A and R115A in Bacillus PS3 ATP synthase increase ATP binding affinity, suggesting broader evolutionary implications for ATP sensing.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- The ε subunit of ATP synthase regulates ATP hydrolysis in bacteria.
- ATP binding affinities of ε subunits vary significantly across bacterial species.
- A previously studied double mutant (R103A/R115A) showed a two-order-of-magnitude increase in ATP binding affinity.
Purpose of the Study:
- To investigate the individual roles of R103A and R115A mutations in Bacillus PS3 ATP synthase.
- To determine the effect of single mutations on ATP binding affinity.
- To explore evolutionary patterns of these mutations in related organisms.
Main Methods:
- Atomic-resolution molecular dynamics simulations.
- Analysis of single point mutations (R103A, R115A).
- Evolutionary analysis of ε subunit sequences.
Main Results:
- Molecular dynamics simulations predict increased ATP binding affinity for both R103A and R115A single mutants.
- Evolutionary analysis identified substitutions at R103 and R115 in other bacillic organisms.
- These findings suggest a conserved mechanism for enhanced ATP binding.
Conclusions:
- Both R103A and R115A single mutations enhance ATP binding affinity in Bacillus PS3 ATP synthase.
- Evolutionary data suggest that other bacillic organisms may possess ε subunits with higher ATP binding affinities.
- These mutations likely play a significant role in bacterial ATP homeostasis.
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