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First look at an enzyme target for antibacterial and cancer drugs
Date:12/20/2007

e taken from yeast as it interacted with a segment of DNA. The images revealed that topo II causes a sharp bend - 150 degrees or more - in the DNA segment at the point where it is cleaved. The near folding-in-half of the DNA segment helps enable topo II to recognize where it should disentangle DNA strands.

Large conformational changes in the topo II accompany the DNA deformation, creating a bipartite catalytic site that positions the DNA backbone near a reactive tyrosine and coordinated magnesium ion, said Berger. Remarkably, this configuration turns out to also closely resemble the catalytic site of certain type I topoisomerases, which reinforces the evolutionary link between what are otherwise structurally and functionally distinct enzymes.

If the DNA in a single set of human chromosomes is stretched out and joined together, it measures about two meters in length. In order to be packed within the tiny confines of a cells nucleus, all of this double-stranded DNA must be tightly bundled by a process known as supercoiling. During mitosis, the process by which a dividing cell duplicates its chromosomes and distributes them equally between two daughter cells, these coils of DNA give rise to knots and jumbles that must be unlinked. Failure to properly do so can give rise to chromosome breaks, which in turn can lead to genome instabilities and cell death.

You can think of DNA in the cell as the ultimate extension cord or set of holiday lights which, no matter how carefully you organize them, inevitably must be unraveled before they can be used, said Berger. Topo II performs this unraveling for DNA in the cell.

Despite the important role and extensive study of topo II, structural information and how the enzyme is able to perform its magic have remained a mystery. The problem was that until the advent of synchrotron light sources such as the ALS, researchers lacked the tools to perform sufficiently high-resolution crystallography. The r
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Contact: Lynn Yarris
lcyarris@lbl.gov
510-486-5375
DOE/Lawrence Berkeley National Laboratory  
Source:Eurekalert

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