Journal
EMBO JOURNAL
Volume 25, Issue 6, Pages 1324-1334Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.emboj.7601018
Keywords
eukaryotic transposition; Tc1/mariner transposon; two-metal active site binding; transposase
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Funding
- Medical Research Council [G0301082] Funding Source: researchfish
- Medical Research Council [G0301082] Funding Source: Medline
- Wellcome Trust [074522] Funding Source: Medline
- MRC [G0301082] Funding Source: UKRI
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We present the crystal structure of the catalytic domain of Mos1 transposase, a member of the Tc1/mariner family of transposases. The structure comprises an RNase H-like core, bringing together an aspartic acid triad to form the active site, capped by N- and C-terminal a-helices. We have solved structures with either one Mg2+ or two Mn2+ ions in the active site, consistent with a two-metal mechanism for catalysis. The lack of hairpin-stabilizing structural motifs is consistent with the absence of a hairpin intermediate in Mos1 excision. We have built a model for the DNA-binding domain of Mos1 transposase, based on the structure of the bipartite DNA-binding domain of Tc3 transposase. Combining this with the crystal structure of the catalytic domain provides a model for the paired-end complex formed between a dimer of Mos1 transposase and inverted repeat DNA. The implications for the mechanisms of first and second strand cleavage are discussed.
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