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MukB acts as a macromolecular clamp in DNA condensation

Nature Structural & Molecular Biology volume 15, pages 411–418 (2008)Cite this article

Abstract

Correct folding of the chromosome into its highly ordered structure requires the action of condensins. The multisubunit condensins are highly conserved from bacteria to humans, and at their core they contain the characteristic V-shaped dimer of structural maintenance of chromosome proteins. The mechanism of DNA rearrangements by condensins remains unclear. Using magnetic tweezers, we show that bacterial condensin MukB acts as an ATP-modulated macromolecular assemblage in DNA condensation. Condensation occurs in a highly cooperative manner, resulting in the formation of force-resilient clusters. ATP regulates nucleation but not propagation of the clusters and seems to play a structural role. MukB clusters can further interact with each other, thereby bringing distant DNA segments together. The resulting activity has not previously been described among DNA-remodeling machines and may explain how the protein can organize the global structure of the chromosome.

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Figure 1: ATP-independent DNA condensation by MukB.
Figure 2: Single steps in DNA condensation and decondensation.
Figure 3: DNA extension during repeated stretch-release cycles of MukB–DNA complex.
Figure 4: Progressive DNA condensation by MukB yields increasingly more resilient complexes.
Figure 5: Condensation occurs cooperatively and is stimulated by ATP.
Figure 6: The web-of-clamps model of chromatin organization.

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Acknowledgements

The authors are indebted to D. Bensimon and V. Croquette for their help and advice in assembling the magnetic tweezers. This work has been supported in part by grant GM63786 from the US National Institutes of Health and an award from the Research Corporation.

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry, University of Oklahoma, 620 Parrington Oval, Norman, 73019, Oklahoma, USA

    Yuanbo Cui, Zoya M Petrushenko & Valentin V Rybenkov

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Contributions

Y.C. carried out analysis of MukB using magnetic tweezers; Z.M.P. purified proteins and verified their biochemical activity; V.V.R. designed experiments and statistical approaches and wrote the manuscript.

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Correspondence to Valentin V Rybenkov.

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Cui, Y., Petrushenko, Z. & Rybenkov, V. MukB acts as a macromolecular clamp in DNA condensation. Nat Struct Mol Biol 15, 411–418 (2008). https://doi.org/10.1038/nsmb.1410

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