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Open and Closed Questions about Open and Closed SMC
1Microbial Genetics Laboratory, Genetic Strains Research Center, National Institute of Genetics, Shizuoka 411-8540, Japan; Department of Genetics, SOKENDAI (The Graduate University for Advanced Studies), Shizuoka 411-8540, Japan.
Structure (London, England : 1993)
|April 6, 2017
Summary
The bacterial condensin complex Smc-ScpAB uses ATP hydrolysis to open and close its tripartite ring, entrapping DNA to separate replicated chromosomes. Kamada et al. reveal the structural dynamics of this ring and its regulatory role in chromosome segregation.
Area of Science:
- Structural biology
- Molecular microbiology
- Biochemistry
Background:
- The bacterial condensin complex Smc-ScpAB is essential for chromosome segregation.
- This complex forms a tripartite ring structure that entraps DNA.
- The opening and closing of the Smc-ScpAB ring are regulated by ATP hydrolysis.
Purpose of the Study:
- To investigate the structural dynamics of the Smc-ScpAB tripartite ring.
- To understand the role of these dynamics in regulating the ring's ATP-dependent cycle.
- To elucidate the mechanism of DNA entrapment and release during chromosome segregation.
Main Methods:
- X-ray crystallography
- Cryo-electron microscopy
- Biochemical assays
Main Results:
- Detailed structural insights into the tripartite ring conformation.
- Identification of key structural transitions during ATP hydrolysis.
- Correlation of structural dynamics with DNA binding and release.
Conclusions:
- The tripartite ring structure of Smc-ScpAB undergoes dynamic conformational changes.
- These structural dynamics are crucial for the ATP-dependent regulation of chromosome segregation.
- Understanding these mechanisms provides insights into DNA management in bacteria.