Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding

Laurie Lannes, Christopher M. Furman, Alison B. Hickman and Fred Dyda ()
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Laurie Lannes: National Institutes of Health
Christopher M. Furman: National Institutes of Health
Alison B. Hickman: National Institutes of Health
Fred Dyda: National Institutes of Health

Nature Communications, 2023, vol. 14, issue 1, 1-18

Abstract: Abstract The Hermes DNA transposon is a member of the eukaryotic hAT superfamily, and its transposase forms a ring-shaped tetramer of dimers. Our investigation, combining biochemical, crystallography and cryo-electron microscopy, and in-cell assays, shows that the full-length Hermes octamer extensively interacts with its transposon left-end through multiple BED domains of three Hermes protomers contributed by three dimers explaining the role of the unusual higher-order assembly. By contrast, the right-end is bound to no BED domains at all. Thus, this work supports a model in which Hermes multimerizes to gather enough BED domains to find its left-end among the abundant genomic DNA, facilitating the subsequent interaction with the right-end.

Date: 2023
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DOI: 10.1038/s41467-023-40210-3

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