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ATP-dependent positive supercoiling of DNA by 13S condensin: a biochemical implication for chromosome condensation.

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Affiliations

  • 1. Cold Spring Harbor Laboratory, New York 11724, USA.
      Authors
    • Kimura K 1
    (1 author)

ORCIDs linked to this article

Cell, 01 Aug 1997, 90(4):625-634
https://doi.org/10.1016/s0092-8674(00)80524-3 PMID: 9288743 

Abstract 

13S condensin is a five-subunit protein complex that plays a central role in mitotic chromosome condensation in Xenopus egg extracts. Two core subunits of this complex, XCAP-C and XCAP-E, belong to an emerging family of putative ATPases, the SMC family. We report here that 13S condensin has a DNA-stimulated ATPase activity and exhibits a high affinity for structured DNAs such as cruciform DNA. 13S condensin is able to introduce positive supercoils into a closed circular DNA in the presence of bacterial or eukaryotic topoisomerase I. The supercoiling reaction is ATP-dependent. We propose that 13S condensin wraps DNA in a right-handed direction by utilizing the energy of ATP hydrolysis. This reaction may represent a key mechanism underlying the compaction of chromatin fibers during mitosis.

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Read article at publisher's site: https://doi.org/10.1016/s0092-8674(00)80524-3

Read article for free, from open access legal sources, via Unpaywall: http://www.cell.com/article/S0092867400805243/pdfUnpaywall

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Funding 

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NIGMS NIH HHS (1)