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Researchers probe a DNA repair enzyme
Date:2/18/2008

dented (for helicases) structural feature an accessory domain stabilized by an iron-sulfur cluster, Spies said.

Working with archaea has the advantage of allowing the researchers to increase the amount available protein and also permits easy genetic manipulation.

Like other helicases, Rad3 is composed of a chain of amino acids. It also contains an ancient prosthetic group called an iron-sulfur cluster, an assembly of four iron and four sulfur atoms incorporated into the protein structure through interaction with four cysteine residues of the amino acid chain.

"DNA helicases, which belong to the Rad3 family, have an auxiliary domain inserted within a conserved motor core. The structure of this domain is stabilized by an iron-sulfur cluster, whose integrity seems to be essential for proper function of these enzymes in DNA repair," Spies said. By mutating the cysteine ligands to the cluster, the researchers probed its role in the molecular mechanism of Rad3 enzymes. Some of these mutations uncoupled DNA translocation and ATP hydrolysis, meaning that the engine of the protein could still use the ATP fuel but was no longer capable of moving along the DNA.

This analysis also revealed that the integrity of the cluster and the iron-containing domain is crucial for recognition of specific DNA structures believed to be physiological targets for this helicase. On making these mutations, the helicase no longer behaves like its supposed to, said graduate student Robert Pugh, lead author on the study. The cluster is still there but the environment around it is somehow changing.


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Contact: Diana Yates
diya@uiuc.edu
217-333-5802
University of Illinois at Urbana-Champaign
Source:Eurekalert  

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