Skip Navigation


Journal of Biochemistry Advance Access originally published online on October 17, 2006
Journal of Biochemistry 2006 140(6):763-776; doi:10.1093/jb/mvj210
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary data
Right arrow All Versions of this Article:
140/6/763    most recent
mvj210v1
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 Request Permissions
Google Scholar
Right arrow Articles by Suetake, I.
Right arrow Articles by Tajima, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Suetake, I.
Right arrow Articles by Tajima, S.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2006 The Japanese Biochemical Society.

ARTICLE

The Amino-Terminus of Mouse DNA Methyltransferase 1 Forms an Independent Domain and Binds to DNA with the Sequence Involving PCNA Binding Motif

Isao Suetake*, Daichika Hayata and Shoji Tajima

Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871

*To whom correspondence should be addressed. Phone: +81-6-6879-8628, Fax: +81-6-6879-8629, E-mail: suetake{at}protein.osaka-u.ac.jp


  Abstract

DNA methylation patterns in genome are maintained during replication by a DNA methyltransferase Dnmt1. Mouse Dnmt1 is a 180 kDa protein comprising the N-terminal regulatory domain, which covers 2/3 of the molecule, and the rest C-terminal catalytic domain. In the present study, we demonstrated that the limited digestion of full-length Dnmt1 with different proteases produced a common N-terminal fragment, which migrated along with Dnmt1 (1–248) in SDS–polyacrylamide gel electrophoresis. Digestion of the N-terminal domains larger than Dnmt1 (1–248) with chymotrypsin again produced the fragment identical to the size of Dnmt1 (1–248). These results indicate that the N-terminal domain of 1–248 forms an independent domain. This N-terminal domain showed DNA binding activity, and the responsible sequence was narrowed to the 79 amino acid residues involving the proliferating cell nuclear antigen (PCNA) binding motif. The DNA binding activity did not distinguish between DNA methylated and non-methylated states, but preferred to bind to the minor groove of AT-rich sequence. The DNA binding activity of the N-terminal domain competed with the PCNA binding. We propose that DNA binding activity of the N-terminal domain contributes to the localization of Dnmt1 to AT-rich sequence such as Line 1, satellite, and the promoter of tissue-specific silent genes.


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
 DevelopmentHome page
D. S. Dunican, A. Ruzov, J. A. Hackett, and R. R. Meehan
xDnmt1 regulates transcriptional silencing in pre-MBT Xenopus embryos independently of its catalytic function
Development, April 1, 2008; 135(7): 1295 - 1302.
[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.