Skip Navigation



Nucleic Acids Research Advance Access published online on May 29, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn333
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (8132K) Freely available
Right arrow Screen PDF (1035K) Freely available
Right arrow Supplementary Data
Right arrowOA All Versions of this Article:
36/12/3939    most recent
gkn333v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Sisáková, E.
Right arrow Articles by Szczelkun, M. D.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sisáková, E.
Right arrow Articles by Szczelkun, M. D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.