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

Julia M. Richardson, Sean D. Colloms, David J. Finnegan, Malcolm D. Walkinshaw

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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.

Original languageEnglish
Pages (from-to)1096-1108
Number of pages13
JournalCell
Volume138
Issue number6
DOIs
Publication statusPublished - 18 Sept 2009

Keywords / Materials (for Non-textual outputs)

  • DNA

Fingerprint

Dive into the research topics of 'Molecular Architecture of the Mos1 Paired-End Complex: The Structural Basis of DNA Transposition in a Eukaryote'. Together they form a unique fingerprint.

Cite this