The large bat Helitron DNA transposase forms a compact monomeric assembly that buries and protects its covalently bound 5 '-transposon end

0547602 - FGÚ 2022 RIV GB eng J - Článek v odborném periodiku
Košek, Dalibor - Grabundzija, I. - Lei, H. - Bilic, I. - Wang, H. - Jin, Y. - Peaslee, G. F. - Hickman, A. B. - Dyda, F.
The large bat Helitron DNA transposase forms a compact monomeric assembly that buries and protects its covalently bound 5 '-transposon end.
Molecular Cell. Roč. 81, č. 20 (2021), s. 4271-4286.e4. ISSN 1097-2765. E-ISSN 1097-4164
Institucionální podpora: RVO:67985823
Klíčová slova: helitron * mobile genetic element * transposon * evolution * SF1B helicase * HUH endonuclease * cryo-EM * transposase * gene delivery * rolling circle mechanism
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 19.328, rok: 2021
Způsob publikování: Omezený přístup
https://doi.org/10.1016/j.molcel.2021.07.028

Helitrons are widespread eukaryotic DNA transposons that have significantly contributed to genome variability and evolution, in part because of their distinctive, replicative rolling-circle mechanism, which often mobilizes adjacent genes. Although most eukaryotic transposases form oligomers and use RNase H-like domains to break and rejoin double-stranded DNA (dsDNA), Helitron transposases contain a single-stranded DNA (ssDNA)-specific HUH endonuclease domain. Here, we report the cryo-electron microscopy structure of a Helitron transposase bound to the 5'-transposon end, providing insight into its multidomain architecture and function. The monomeric transposase forms a tightly packed assembly that buries the covalently attached cleaved end, protecting it until the second end becomes available. The structure reveals unexpected architectural similarity to Tral, a bacterial relaxase that also catalyzes ssDNA movement. The HUH active site suggests how two juxtaposed tyrosines, a feature of many replication initiators that use HUH nucleases, couple the conformational shift of an alpha-helix to control strand cleavage and ligation reactions.
Trvalý link: http://hdl.handle.net/11104/0323811