English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Formation of nucleoprotein filaments by mammalian DNA methyltransferase Dnmt3a in complex with regulator Dnmt3L

Jurkowska, R. Z., Anspach, N., Urbanke, C., Jia, D., Reinhardt, R., Nellen, W., et al. (2008). Formation of nucleoprotein filaments by mammalian DNA methyltransferase Dnmt3a in complex with regulator Dnmt3L. Nucleic Acids Research, 36(21), 6656-6663. Retrieved from 10.1093/nar/gkn747.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Nucleic Acids Res

Files

show Files
hide Files
:
6656.pdf (Any fulltext), 4MB
Name:
6656.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
eDoc_access: PUBLIC
License:
-

Locators

show

Creators

show
hide
 Creators:
Jurkowska, Renata Z., Author
Anspach, Nils, Author
Urbanke, Claus, Author
Jia, Da, Author
Reinhardt, Richard1, Author           
Nellen, Wolfgang, Author
Cheng, Xiaodong, Author
Jeltsch, Albert, Author
Affiliations:
1High Throughput Technologies, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433552              

Content

show
hide
Free keywords: -
 Abstract: The C-terminal domains of Dnmt3a and Dnmt3L form elongated heterotetramers (3L-3a-3a-3L). Analytical ultracentrifugation confirmed the Dnmt3a-C/3L-C complex exists as a 2:2 heterotetramer in solution. The 3a-3a interface is the DNA-binding site, while both interfaces are essential for AdoMet binding and catalytic activity. Hairpin bisulfite analysis shows correlated methylation of two CG sites in a distance of approximately 8-10 bp in the opposite DNA strands, which corresponds to the geometry of the two active sites in one Dnmt3a-C/3L-C tetramer. Correlated methylation was also observed for two CG sites at similar distances in the same DNA strand, which can be attributed to the binding of two tetramers next to each other. DNA-binding experiments show that Dnmt3a-C/3L-C complexes multimerize on the DNA. Scanning force microscopy demonstrates filament formation rather than binding of single tetramers and shows that protein-DNA filament formation leads to a 1.5-fold shortening of the DNA length.

Details

show
hide
Language(s): eng - English
 Dates: 2008-10-22
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 413817
URI: 10.1093/nar/gkn747
URI: 10.1093/nar/gkn747
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nucleic Acids Research
  Alternative Title : Nucleic Acids Res
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 36 (21) Sequence Number: - Start / End Page: 6656 - 6663 Identifier: ISSN: 0305-1048