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

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.

SUBMITTER: Lannes L

PROVIDER: S-EPMC10368747 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature

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

Lannes Laurie L Furman Christopher M CM Hickman Alison B AB Dyda Fred F

Nature communications 20230725 1

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-en ...[more]

PMID: 37491363

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