A proposed mechanism for IS607-family serine transposases

Boocock, M.R. and Rice, P.A. (2013) A proposed mechanism for IS607-family serine transposases. Mobile DNA, 4(24), (doi: 10.1186/1759-8753-4-24)

[img]
Preview
Text
88805.pdf - Published Version
Available under License Creative Commons Attribution.

1MB

Abstract

Background The transposases encoded by the IS607 family of mobile elements are unusual serine recombinases with an inverted domain order and minimal specificity for target DNA.<p></p> Results Structural genomics groups have determined three crystal structures of the catalytic domains of IS607 family transposases. The dimers formed by these catalytic domains are very different from those seen for other serine recombinases and include interactions that usually only occur upon formation of a synaptic tetramer.<p></p> Conclusions Based on these structures, we propose a model for how IS607-family transposases could form a synaptic tetramer. The model suggests that, unlike other serine recombinases, these enzymes carry out sequence-specific DNA binding and catalysis in trans: the DNA binding and catalytic domains of each subunit are proposed to interact with different DNA duplexes. The model also suggests an explanation for the minimal target DNA specificity.<p></p>

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Boocock, Dr Martin
Authors: Boocock, M.R., and Rice, P.A.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:Mobile DNA
Publisher:BioMed Central
ISSN:1759-8753
ISSN (Online):1759-8753
Copyright Holders:Copyright © 2013 The Authors
First Published:First published in Mobile DNA 4:24
Publisher Policy:Reproduced under a Creative Commons License

University Staff: Request a correction | Enlighten Editors: Update this record