Mechanism for nuclease regulation in RecBCD.

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Title: Mechanism for nuclease regulation in RecBCD.
Authors: Wilkinson, M
Chaban, Y
Wigley, DB
Item Type: Journal Article
Abstract: In bacterial cells, processing of double-stranded DNA breaks for repair by homologous recombination is catalysed by AddAB, AdnAB or RecBCD-type helicase-nucleases. These enzyme complexes are highly processive, duplex unwinding and degrading machines that require tight regulation. Here, we report the structure of E.coli RecBCD, determined by cryoEM at 3.8 Å resolution, with a DNA substrate that reveals how the nuclease activity of the complex is activated once unwinding progresses. Extension of the 5’-tail of the unwound duplex induces a large conformational change in the RecD subunit, that is transferred through the RecC subunit to activate the nuclease domain of the RecB subunit. The process involves a SH3 domain that binds to a region of the RecB subunit in a binding mode that is distinct from others observed previously in SH3 domains and, to our knowledge, this is the first example of peptide-binding of an SH3 domain in a bacterial system.
Issue Date: 20-Sep-2016
Date of Acceptance: 29-Aug-2016
ISSN: 2050-084X
Publisher: eLife Sciences Publications
Journal / Book Title: eLife
Volume: 5
Copyright Statement: Copyright Wilkinson et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.
Sponsor/Funder: Wellcome Trust
Cancer Research UK
Medical Research Council (MRC)
Funder's Grant Number: 095519/B/11/Z
Publication Status: Published
Open Access location:
Article Number: e18227
Appears in Collections:Department of Medicine

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