Imperial College London
Alternate

Professor Dale Wigley FRS

Faculty of Medicine, Department of Infectious Disease

Chair in Protein Crystallography
 
 
 
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Contact

 

+44 (0)20 7594 8417d.wigley

 
 
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Assistant

 

Miss Kelly Butler +44 (0)20 7594 2763

 
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Location

 

258Sir Alexander Fleming BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Krajewski:2014:10.1038/nature13037,
author = {Krajewski, WW and Fu, X and Wilkinson, M and Cronin, NB and Dillingham, MS and Wigley, DB},
doi = {10.1038/nature13037},
journal = {Nature},
pages = {416--419},
title = {Structural basis for translocation by AddAB helicase–nuclease and its arrest at χ sites},
url = {http://dx.doi.org/10.1038/nature13037},
volume = {508},
year = {2014}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - In bacterial cells, processing of double-stranded DNA breaks for repair by homologous recombination is dependent upon the recombination hotspot sequence χ (Chi)1,2 and is catalysed by either an AddAB- or RecBCD-type helicase–nuclease (reviewed in refs 3, 4). These enzyme complexes unwind and digest the DNA duplex from the broken end until they encounter a χ sequence5, whereupon they produce a 3′ single-stranded DNA tail onto which they initiate loading of the RecA protein6. Consequently, regulation of the AddAB/RecBCD complex by χ is a key control point in DNA repair and other processes involving genetic recombination. Here we report crystal structures of Bacillus subtilis AddAB in complex with different χ-containing DNA substrates either with or without a non-hydrolysable ATP analogue. Comparison of these structures suggests a mechanism for DNA translocation and unwinding, suggests how the enzyme binds specifically to χ sequences, and explains how χ recognition leads to the arrest of AddAB (and RecBCD) translocation that is observed in single-molecule experiments7,8,9.
AU  - Krajewski,WW
AU  - Fu,X
AU  - Wilkinson,M
AU  - Cronin,NB
AU  - Dillingham,MS
AU  - Wigley,DB
DO  - 10.1038/nature13037
EP  - 419
PY  - 2014///
SN  - 0028-0836
SP  - 416
TI  - Structural basis for translocation by AddAB helicase–nuclease and its arrest at χ sites
T2  - Nature
UR  - http://dx.doi.org/10.1038/nature13037
UR  - https://www.nature.com/articles/nature13037
UR  - http://hdl.handle.net/10044/1/59806
VL  - 508
ER  -
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