@article{Wilkinson:2016:10.7554/eLife.18227,
author = {Wilkinson, M and Chaban, Y and Wigley, DB},
doi = {10.7554/eLife.18227},
journal = {eLife},
title = {Mechanism for nuclease regulation in RecBCD.},
url = {http://dx.doi.org/10.7554/eLife.18227},
volume = {5},
year = {2016}
}

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TY  - JOUR
AB  - 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.
AU  - Wilkinson,M
AU  - Chaban,Y
AU  - Wigley,DB
DO  - 10.7554/eLife.18227
PY  - 2016///
SN  - 2050-084X
TI  - Mechanism for nuclease regulation in RecBCD.
T2  - eLife
UR  - http://dx.doi.org/10.7554/eLife.18227
UR  - http://hdl.handle.net/10044/1/40778
VL  - 5
ER  - 

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