Skip Navigation

This Article
Right arrow Print PDF (1000K)
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 (39)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Laayoun, A.
Right arrow Articles by Smith, S. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Laayoun, A.
Right arrow Articles by Smith, S. S.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1995, Vol. 23, No. 9 1584-1589
© 1995


ENZYMOLOGY

Methylation of slipped duplexes, snapbacks and cruciforms by human DNA(cytosine-5)methyltransferase

All Laayoun* and Steven S. Smith

Department of Cell and Tumor Biology, City of Hope National Medical Center 1500 E. Duarte Road, Duarte, CA 91010, USA

* To whom correspondence should be addressed at present address: Laboratoire des Sondes Nucléiques, UMR bio-Mérieux, CNRS n° 103, Ecole Normale Supérieure, 46 allée d'ltalic, 69364 Lyon cedex 07, France

Received December 9, 1994. Revised March 16, 1995. Accepted March 16, 1995.

When human DNA(cytosine-5)methyttransferase was rused to methylate a series of snapback ollgodeoxy-nucleotides of differing stem lengths, each containing a centrally located CG dinucleotlde recognition site, the enzyme required a minimum of 22 base pairs in the stem for maximum activity. Extrahelical cytosines In slipped duplexes that were 30 base pairs In length acted as effective methyl acceptors and were more rapidly methylated than cytosines that were Watson-Crick paired. Duplexes containing hairpins of CCG repeats in cruciform structures in which the enzyme recognition sequence was disrupted by a C.C mispair were also more rapidly methylated than control Wat-son-Crlck-paired duplexes. Since enzymes have higher affinities for their transition states than for their substrates, the results with extrahelical and mispaired cytosines suggest that these structures can be viewed as analogs of the transition state intermediates produced during catalysis by methyltransferases.


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
Hum Mol GenetHome page
S. Al-Mahdawi, R. M. Pinto, O. Ismail, D. Varshney, S. Lymperi, C. Sandi, D. Trabzuni, and M. Pook
The Friedreich ataxia GAA repeat expansion mutation induces comparable epigenetic changes in human and transgenic mouse brain and heart tissues
Hum. Mol. Genet., March 1, 2008; 17(5): 735 - 746.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
A. Bird
DNA methylation patterns and epigenetic memory
Genes & Dev., January 1, 2002; 16(1): 6 - 21.
[Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Pradhan, A. Bacolla, R. D. Wells, and R. J. Roberts
Recombinant Human DNA (Cytosine-5) Methyltransferase. I. EXPRESSION, PURIFICATION, AND COMPARISON OF DE NOVO AND MAINTENANCE METHYLATION
J. Biol. Chem., November 12, 1999; 274(46): 33002 - 33010.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
R. Singal and G. D. Ginder
DNA Methylation
Blood, June 15, 1999; 93(12): 4059 - 4070.
[Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
M. Stam, A. Viterbo, J. N. M. Mol, and J. M. Kooter
Position-Dependent Methylation and Transcriptional Silencing of Transgenes in Inverted T-DNA Repeats: Implications for Posttranscriptional Silencing of Homologous Host Genes in Plants
Mol. Cell. Biol., November 1, 1998; 18(11): 6165 - 6177.
[Abstract] [Full Text]


Home page
Proc. Natl. Acad. Sci. USAHome page
S. S. Smith, L. Niu, D. J. Baker, J. A. Wendel, S. E. Kane, and D. S. Joy
Nucleoprotein-based nanoscale assembly
PNAS, March 18, 1997; 94(6): 2162 - 2167.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
G. Vilkaitis, E. Merkiene, S. Serva, E. Weinhold, and S. Klimasauskas
The Mechanism of DNA Cytosine-5 Methylation. KINETIC AND MUTATIONAL DISSECTION OF HhaI METHYLTRANSFERASE
J. Biol. Chem., June 8, 2001; 276(24): 20924 - 20934.
[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.