An iron-sulfur cluster is essential for the binding of broken DNA by AddAB-type helicase-nucleases.
作者： Joseph T. P. Yeeles , Richard Cammack , Mark S. Dillingham
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摘要: The bacterial helicase-nuclease complex AddAB converts double-stranded DNA breaks into substrates for RecA-dependent recombinational repair. Here we show that the AddB subunit contains a novel class of nuclease domain distinguished by presence an iron-sulfur cluster. cluster is coordinated unusual arrangement cysteine residues originate from both sides nuclease, forming “iron staple” required local structural integrity this domain. Disruption mutagenesis eliminates ability to bind duplex ends without affecting single-stranded DNA-dependent ATPase activity. Sequence analysis suggests related iron staple present in eukaryotic replication/repair factor Dna2, where it also associated with helicase motor.
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