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Mechanism of Mos1 transposition: insights from structural analysis

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)1324-1334
Number of pages11
JournalEMBO Journal
Volume25
Issue number6
DOIs
Publication statusPublished - 22 Mar 2006

Abstract

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.

    Research areas

  • eukaryotic transposition , Tc1/mariner transposon , two-metal active site binding , transposase

ID: 1772765