Abstract
Human DNA helicase B (HELB) is a poorly-characterised helicase suggested to play several functions in DNA metabolism including the stimulation of RAD51-mediated 5′-3′ heteroduplex extension to promote homologous recombination (HR). Most recently, and in apparent contradiction to the role in the stimulation of HR, HELB was proposed to inhibit HR by antagonising the processive resection nucleases EXO1 and DNA2/BLM. In this work, we used bulk and single molecule approaches to characterise the biochemical activities of HELB protein with a particular focus on its interactions with RPA and RPA-ssDNA filaments.
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