西亚试剂：Molecular Architecture of the Mos1 Paired-End Complex: The

Molecular Architecture of the Mos1 Paired-End Complex: The Structural Basis of DNA Transposition in a Eukaryote

Julia M. Richardson1,Sean D. Colloms2, David J. Finnegan1 and Malcolm D. Walkinshaw1

1School of Biological Sciences, University of Edinburgh, The King's Buildings, Mayfield Road, Edinburgh, EH9 3JR, Scotland
2Xermit, 44 Colchester Drive, Glasgow, G12 0NF, Scotland

A key step in cut-and-paste DNA transposition is the pairing of transposon ends before the element is excised and inserted at a new site in its host genome. Crystallographic analyses of the paired-end complex (PEC) formed from precleaved transposon ends and the transposase of the eukaryotic element Mos1 reveals two parallel ends bound to a dimeric enzyme. The complex has a trans arrangement, with each transposon end recognized by the DNA binding region of one transposase monomer and by the active site of the other monomer. Two additional DNA duplexes in the crystal indicate likely binding sites for flanking DNA. Biochemical data provide support for a model of the target capture complex and identify Arg186 to be critical for target binding. Mixing experiments indicate that a transposase dimer initiates first-strand cleavage and suggest a pathway for PEC formation.

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