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Usp7 and Uhrf1 control ubiquitination and stability of the maintenance DNA methyltransferase Dnmt1
Author(s) -
Qin Weihua,
Leonhardt Heinrich,
Spada Fabio
Publication year - 2011
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.22998
Subject(s) - dnmt1 , dna methyltransferase , ubiquitin , dna methylation , ubiquitin ligase , biology , methyltransferase , methylation , microbiology and biotechnology , dna , chemistry , biochemistry , gene , gene expression
In mammals Dnmt1 is the DNA methyltransferase chiefly responsible for maintaining genomic methylation patterns through DNA replication cycles, but how its maintenance activity is controlled is still not well understood. Interestingly, Uhrf1, a crucial cofactor for maintenance of DNA methylation by Dnmt1, is endowed with E3 ubiquitin ligase activity. Here, we show that both Dnmt1 and Uhrf1 coprecipitate with ubiquitin specific peptidase 7 (Usp7), a de‐ubiquitinating enzyme. Overexpression of Uhrf1 and Usp7 resulted in opposite changes in the ubiquitination status and stability of Dnmt1. Our findings suggest that, by balancing Dnmt1 ubiquitination, Usp7 and Uhrf1 fine tune Dnmt1 stability. J. Cell. Biochem. 112: 439–444, 2011. © 2010 Wiley‐Liss, Inc.