Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding
Year: 2023
Type: article
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.
Source: Nature Communications
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $6,290
Funders: U.S. Department of Energy, U.S. Department of Health and Human Services, National Institutes of Health, Office of Science, National Heart, Lung, and Blood Institute, National Institute of Diabetes and Digestive and Kidney Diseases, National Center for Research Resources, Basic Energy Sciences, Argonne National Laboratory
Awards: G1633006425, G1678787968, G1756342139, G1800737955, G18202666, Phase II SER-CAT Optimization: Acquisition of a next generation area detector, G2123841078, G3100170572, G3338542329, Acquisition of a High Precision Micro Diffractometer to Support NIH funded Research at SER-CAT, G3522124907, Structure and function of eukaryotic DNA transposases, G434509735, G572720644, G5921955326, G6800544485, G760289873, G7932540327, G8054752631, G9000018190, Acquition of a microdiffractometer for SER-CAT
OpenAlex ID: W4385233057