期刊
BIOCHEMICAL JOURNAL
卷 405, 期 -, 页码 369-378出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20061873
关键词
chromobox 4 (Cbx4); DNA methyltransferase 3a (Dnmt3a); E3 ligase; small ubiquitin-related modifier (SUMO); SUMOylation; Pro-Trp-Trp-Pro domain (PWWP domain)
The 'de novo methyltransferase' Dnmt3a (DNA methyltransferase 3a) has been shown to mediate transcriptional repression. Posttranslational modification of Dnmt3a by SUMOylation affects its ability to transcriptionally repress. However, very little is known about how the SUMOylation process is regulated. In the present study, we identified a PcG (Polycomb group) protein, Cbx4 (chromobox 4), as a specific interaction partner of Dnmt3a. Co-expression of Cbx4 and SUMO-1 (small ubiquitin-related modifier-1) along with Dnmt3a in transfected cells results in enhanced modification of Dnmt3a with SUMO-1. Purified Cbx4 also promotes SUMOylation of Dnmt3a in vitro. The modification occurs in the N-terminal regulatory region, including the PWWP (Pro-Trp-Trp-Pro) domain. Our results suggest that Cbx4 functions as a SUMO E3 ligase for Dnmt3a and it might be involved in the functional regulation of DNA methyltransferases by promoting their SUMO modification.
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