Skip Navigation

This Article
Right arrow Print PDF (265K)
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 Search for citing articles in:
ISI Web of Science (26)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Belogurov, A. A.
Right arrow Articles by Delver, E. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Belogurov, A. A.
Right arrow Articles by Delver, E. P.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1995, Vol. 23, No. 5 785-787
© 1995

ENZYMOLOGY

A motif conserved among the type I restriction-modification enzymes and antirestriction proteins: a possible basis for mechanism of action of plasmid-encoded antirestriction functions

Anatol A. Belogurov* and Eugene P. Delver

Department of Genetic Engineering, Cardiology Research Center Moscow 121552, Russia

*To whom correspondence should be addressed

Received November 14, 1994. Revised January 19, 1995. Accepted January 19, 1995.

Antirestriction proteins Ard encoded by some self-transmissible plasmids specifically inhibit restriction by members ofall three families of type I restriction-modification (R-M) systems in E.coli. Recently, we have identified the amino acid region, ‘antirestriction’ domain, that is conserved within different plasmid and phage T7-encoded antirestriction proteins and may be involved in interaction with the type I R-M systems. In this paper we demonstrate that this amino acid sequence shares considerable similarity with a well-known conserved sequence (the Argos repeat) found in the DNA sequence specificity (S) polypeptides of type I systems. We suggest that the presence of these similar motifs in restriction and antirestriction proteins may give a structural basis for their interaction and that the antirestriction action of Ard proteins may be a result of the competition between the ‘antirestriction’ domains of Ard proteins and the similar conserved domains of the S subunits that are believed to play a role In the subunit assembly of type I R-M systems.


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


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
S. A. McMahon, G. A. Roberts, K. A. Johnson, L. P. Cooper, H. Liu, J. H. White, L. G. Carter, B. Sanghvi, M. Oke, M. D. Walkinshaw, et al.
Extensive DNA mimicry by the ArdA anti-restriction protein and its role in the spread of antibiotic resistance
Nucleic Acids Res., August 1, 2009; 37(15): 4887 - 4897.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
A. T. Thomas, W. J. Brammar, and B. M. Wilkins
Plasmid R16 ArdA Protein Preferentially Targets Restriction Activity of the Type I Restriction-Modification System EcoKI
J. Bacteriol., March 15, 2003; 185(6): 2022 - 2025.
[Abstract] [Full Text] [PDF]

Home page
 MicrobiologyHome page
N. E. Murray
Immigration control of DNA in bacteria: self versus non-self
Microbiology, January 1, 2002; 148(1): 3 - 20.
[Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
C. Atanasiu, O. Byron, H. McMiken, S. S. Sturrock, and D. T. F. Dryden
Characterisation of the structure of ocr, the gene 0.3 protein of bacteriophage T7
Nucleic Acids Res., July 15, 2001; 29(14): 3059 - 3068.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
N. E. Murray
Type I Restriction Systems: Sophisticated Molecular Machines (a Legacy of Bertani and Weigle)
Microbiol. Mol. Biol. Rev., June 1, 2000; 64(2): 412 - 434.
[Abstract] [Full Text] [PDF]


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.