Skip Navigation

This Article
Right arrow Print PDF (1095K)
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 Smith, D. W.
Right arrow Articles by Reich, N. O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Smith, D. W.
Right arrow Articles by Reich, N. O.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1992, Vol. 20, No. 22 6091-6096
© 1992

ENZYMOLOGY

In vivo specificity of EcoRI DNA methyltransferase

Dean W. Smith, Scott W. Crowder and Norbert O. Reich*

Department of Chemistry, University of California Santa Barbara, CA 93106, USA

* To whom correspondence should be addressed

Received March 4, 1992. Revised October 16, 1992. Accepted October 16, 1992.

The EcoRI adenine DNA methyltransferase forms par of a bacterial restriction/modification system; thi methyltransferase modifies the second adenine withii the canonical site GAATTC, thereby preventing thi EcoRI endonuclease from cleaving this site. We shov that five noncanonical EcoRI sites (TAATTC, CAATTC GTATTC, GGATTC and GAGTTC) are not methylate in vivo under conditions when the canonical site ii methylated. Only when the methyltransferase ii overexpressed is partial in vivo methylation of the fivi sites detected. Our results suggest that thi methyltransferase does not protect host DNA agains potential endonuclease-mediated cleavage a noncanonical sites. Our related in vitro analysis of thi methyltransferase reveals a low level of sequence discrimination. We propose that the high in vivo specificity may be due to the active removal of methylated sequences by DNA repair enzymes (J Bacteriology (1987), 169 3243–3250).


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. S. Szegedi and R. I. Gumport
DNA binding properties in vivo and target recognition domain sequence alignment analyses of wild-type and mutant RsrI [N6-adenine] DNA methyltransferases
Nucleic Acids Res., October 15, 2000; 28(20): 3972 - 3981.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
W. M. Lindstrom Jr., J. Flynn, and N. O. Reich
Reconciling Structure and Function in HhaI DNA Cytosine-C-5 Methyltransferase
J. Biol. Chem., February 18, 2000; 275(7): 4912 - 4919.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. W. Allan, R. Garcia, K. Maegley, J. Mort, D. Wong, W. Lindstrom, J. M. Beechem, and N. O. Reich
DNA Bending by EcoRI DNA Methyltransferase Accelerates Base Flipping but Compromises Specificity
J. Biol. Chem., July 2, 1999; 274(27): 19269 - 19275.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. Bandaru, J. Gopal, and A. S. Bhagwat
Overproduction of DNA Cytosine Methyltransferases Causes Methylation and C [IMAGE] T Mutations at Non-canonical Sites
J. Biol. Chem., March 29, 1996; 271(13): 7851 - 7859.
[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.