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-Structure paper
タイトル | Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 4470, Year 2023 |
掲載日 | 2023年7月25日 |
著者 | Laurie Lannes / Christopher M Furman / Alison B Hickman / Fred Dyda / |
PubMed 要旨 | 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- ...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. |
リンク | Nat Commun / PubMed:37491363 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.5 - 5.1 Å |
構造データ | EMDB-28034, PDB-8edg: EMDB-40553, PDB-8sjd: PDB-8eb5: |
化合物 | ChemComp-ZN: ChemComp-HOH: |
由来 |
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キーワード | DNA BINDING PROTEIN/DNA / BED domain / zinc-binding domain / transposase / DNA BINDING PROTEIN-DNA complex / RECOMBINATION/DNA / transpososome / protein-DNA complex / RECOMBINATION / RECOMBINATION-DNA complex |