Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX–DNMT3–DNMT3L domain-Reference-Cited by-同舟云学术

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Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX–DNMT3–DNMT3L domain

Published:2009-10-16 Issue:11 Volume:10 Page:1235-1241
ISSN:1469-221X
Container-title:EMBO reports
language:en
Short-container-title:EMBO Rep

Author:

Otani Junji¹,Nankumo Toshiyuki²,Arita Kyohei¹,Inamoto Susumu³,Ariyoshi Mariko¹,Shirakawa Masahiro¹

Affiliation:

1. Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto‐Daigaku Katsura Nishikyo‐Ku Kyoto 615‐8510 Japan

2. Department of Supramolecular Biology, Yokohama City University 1‐7‐29 Suehiro‐cho Tsurumi‐ku Yokohama 230‐0045 Japan

3. Department of Human Genome Research, Kazusa DNA Research Institute 2‐6‐7 Kazusa‐Kamatari Kisarazu Chiba 292‐0818 Japan

Publisher

EMBO

Subject

Genetics,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1038/embor.2009.218

Reference24 articles.

1. Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX

2. HP1-β mobilization promotes chromatin changes that initiate the DNA damage response

3. DNA methylation patterns and epigenetic memory

4. Characterization of sequences associated with position-effect variegation at pericentric sites in Drosophila heterochromatin

5. G9a and HP1 Couple Histone and DNA Methylation to TNFα Transcription Silencing during Endotoxin Tolerance

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