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Nucleic Acids Research Advance Access originally published online on May 29, 2008
Nucleic Acids Research 2008 36(12):3939-3949; doi:10.1093/nar/gkn333
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Nucleic Acids Research, 2008, Vol. 36, No. 12 3939-3949
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

A RecB-family nuclease motif in the Type I restriction endonuclease EcoR124I

Eva Sisáková1, Louise K. Stanley2, Marie Weiserová1 and Mark D. Szczelkun2,*

1Institute of Microbiology v.v.i., Academy of Sciences of the Czech Republic, Prague, Czech Republic and 2DNA-Protein Interactions Unit, Department of Biochemistry, University of Bristol, Bristol, BS8 1TD, UK

*To whom correspondence should be addressed. Tel: +44 117 331 2158; Fax: +44 117 331 2168; Email: mark.szczelkun{at}bristol.ac.uk

Received April 10, 2008. Revised April 30, 2008. Accepted May 8, 2008.

The Type I restriction-modification enzyme EcoR124I is an ATP-dependent endonuclease that uses dsDNA translocation to locate and cleave distant non-specific DNA sites. Bioinformatic analysis of the HsdR subunits of EcoR124I and related Type I enzymes showed that in addition to the principal PD-(E/D)xK Motifs, I, II and III, a QxxxY motif is also present that is characteristic of RecB-family nucleases. The QxxxY motif resides immediately C-terminal to Motif III within a region of predicted {alpha}-helix. Using mutagenesis, we examined the role of the Q and Y residues in DNA binding, translocation and cleavage. Roles for the QxxxY motif in coordinating the catalytic residues or in stabilizing the nuclease domain on the DNA are discussed.

Present address: Louise K. Stanley, Institute of Human Genetics, Molecular Genetics, International Centre for Life, Central Parkway, Newcastle Upon Tyne, NE1 3BZ, UK


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