Structural highlights
Function
Q25438_MUSDO
Publication Abstract from PubMed
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.
Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding.,Lannes L, Furman CM, Hickman AB, Dyda F Nat Commun. 2023 Jul 25;14(1):4470. doi: 10.1038/s41467-023-40210-3. PMID:37491363[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lannes L, Furman CM, Hickman AB, Dyda F. Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding. Nat Commun. 2023 Jul 25;14(1):4470. PMID:37491363 doi:10.1038/s41467-023-40210-3
