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Dynamic coupling between conformations and nucleotide states in DNA gyrase
Aakash Basu1,2,3, Matthew Hobson3,4, Paul Lebel1,2,5
1Department of Applied Physics, Stanford University, Stanford, CA, USA.
Nature Chemical Biology
|April 18, 2018
Summary
Bacterial gyrase uses ATP to wrap DNA, with ADP exchange driving the key remodeling step. ATP hydrolysis then facilitates DNA passage and enzyme resetting, linking gene expression to cellular energy.
Area of Science:
- Molecular biology
- Biochemistry
- Structural biology
Background:
- DNA gyrase is a crucial bacterial enzyme that regulates DNA topology through supercoiling.
- Understanding its mechanism requires mapping structural changes to the ATP nucleotide cycle.
Purpose of the Study:
- To elucidate the coupling mechanisms between DNA manipulation and ATP turnover in E. coli gyrase.
- To investigate the roles of ATP binding, hydrolysis, and product release in gyrase function.
Main Methods:
- Single-molecule tracking of DNA rotation and contraction.
- Analysis of gyrase activity under varied nucleotide conditions (ATP, ADP).
Main Results:
- ATP binding and ADP release are essential for the rate-limiting DNA wrapping transition.
- ATP hydrolysis accelerates DNA strand passage and enzyme resetting.
- Gyrase activity is modulated by nucleotide availability, suggesting a link to cellular energy levels.
Conclusions:
- Gyrase coordinates DNA rearrangements with its ATP-driven protein gate dynamics.
- The enzyme minimizes futile ATP hydrolysis cycles.
- Gyrase activity regulation may link gene expression to cellular metabolism.
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