Structural basis of transposon end recognition explains central features of Tn7 transposition systems.
Structural basis of transposon end recognition explains central features of Tn7 transposition systems.
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DOI:
10.1016/j.molcel.2022.05.005
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发表时间:
2022-07-21
期刊:
影响因子:
16
通讯作者:
Nowotny, Marcin
中科院分区:
文献类型:
--
作者:
Kaczmarska, Zuzanna;Czarnocki-Cieciura, Mariusz;Gorecka-Minakowska, Karolina M.;Wingo, Robert J.;Jackiewicz, Justyna;Zajko, Weronika;Poznanski, Jaroslaw T.;Rawski, Michal;Grant, Timothy;Peters, Joseph E.;Nowotny, Marcin
Tn7 is a bacterial transposon with relatives containing element-encoded CRISPR-Cas systems mediating RNA-guided transposon insertion. Here, we present the 2.7 Å cryoelectron microscopy structure of prototypic Tn7 transposase TnsB interacting with the transposon end DNA. When TnsB interacts across repeating binding sites, it adopts a beads-on-a-string architecture, where the DNA-binding and catalytic domains are arranged in a tiled and intertwined fashion. The DNA-binding domains form few base-specific contacts leading to a binding preference that requires multiple weakly conserved sites at the appropriate spacing to achieve DNA sequence specificity. TnsB binding imparts differences in the global structure of the protein-bound DNA ends dictated by the spacing or overlap of binding sites explaining functional differences in the left and right ends of the element. We propose a model of the strand-transfer complex in which the terminal TnsB molecule is rearranged so that its catalytic domain is in a position conducive to transposition. Kaczmarska et al. present a structure of Tn7 transposon transposase TnsB bound to transposon end DNA. Tn7 is a bacterial transposon. Its relatives containing CRISPR-Cas machinery are promising tools for gene editing. TnsB molecules interact with repeating binding sites in the transposon end in an intertwined fashion for specific end recognition.
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发表时间:
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影响因子:
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