Molecular architecture of the Mos1 paired-end complex: the structural basis of DNA transposition in a eukaryote

Richardson, J.M., Colloms, S.D. , Finnegan, D.J. and Walkinshaw, M.D. (2009) Molecular architecture of the Mos1 paired-end complex: the structural basis of DNA transposition in a eukaryote. Cell, 138(6), pp. 1096-1108. (doi:10.1016/j.cell.2009.07.012)

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Abstract

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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Colloms, Dr Sean
Authors: Richardson, J.M., Colloms, S.D., Finnegan, D.J., and Walkinshaw, M.D.
Subjects:Q Science > QH Natural history > QH345 Biochemistry
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Cell
ISSN:0092-8674
ISSN (Online):1097-4172
Published Online:17 September 2009

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Project CodeAward NoProject NamePrincipal InvestigatorFunder's NameFunder RefLead Dept
252332Interactions between Proteins Bound at Distant Sites on DNA Molecules: Involvement in Site-Specific Recombination ...Sean CollomsWellcome Trust (WELLCOME)57651Institute of Molecular Cell and Systems Biology