The zinc-binding motif of human RECQ5beta suppresses the intrinsic strand-annealing activity of its DExH helicase domain and is essential for the helicase activity of the enzyme

Ren, H; Dou, S X; Zhang, X D; Wang, P Y; Kanagaraj, R; Liu, J L; Janscak, Pavel; Hu, J S; Xi, X G

doi:10.5167/uzh-3850

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Ren, H., Dou, S. X., Zhang, X. D., Wang, P. Y., Kanagaraj, R., Liu, J. L., Janscak, P., Hu, J. S., & Xi, X. G. (2008). The zinc-binding motif of human RECQ5beta suppresses the intrinsic strand-annealing activity of its DExH helicase domain and is essential for the helicase activity of the enzyme. Biochemical Journal, 412, 425–433. https://doi.org/10.1042/BJ20071150

Abstract

RecQ family helicases, functioning as caretakers of genomic integrity, contain a zinc-binding motif which is highly conserved among these helicases, but does not have a substantial structural similarity with any other known zinc-finger folds. In the present study, we show that a truncated variant of the human RECQ5beta helicase comprised of the conserved helicase domain only, a splice variant named RECQ5alpha, possesses neither ATPase nor DNA-unwinding activities, but surprisingly displays a strong strand-annealing activity. In contra