Esco2 is a novel corepressor that associates with various chromatin modifying enzymes

被引:31
作者
Kim, Beorn-Jun [1 ]
Kang, Kyung-Min [1 ]
Jung, Sung Yun [4 ]
Choi, Hyun-Kyung [1 ]
Seo, Jong-Hun [1 ]
Chae, Ji-Hye [1 ]
Cho, Eun-Jung [2 ]
Youn, Hong-Duk [3 ]
Qin, Jun [4 ]
Kim, Seong-Tae [1 ]
机构
[1] Sungkyunkwan Univ, Sch Med, Dept Mol Cell Biol, Suwon 440746, Kyonggi Do, South Korea
[2] Sungkyunkwan Univ, Coll Pharm, Dept Biochem & Mol Biol, Suwon 440746, South Korea
[3] Seoul Natl Univ, Coll Med, Canc Res Inst, Dept Biochem & Mol Biol, Seoul 110799, South Korea
[4] Baylor Coll Med, Verna & Marrs McLean Dept Biochem & Mol Biol, Houston, TX 77030 USA
关键词
Esco2; cohesion; LSD1; CoREST; methylation;
D O I
10.1016/j.bbrc.2008.05.056
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
Accurate chromosome segregation during cell division requires that sister chromatids are kept together by cohesin complex until anaphase, when the chromatids separate and distribute to the two daughter cells. Esco2 is an acetyl transferase that is required for the establishment of sister chromatid cohesion during S phase. Here, we report that Esco2 interacts with several component proteins of the CoREST complex, including a transcription corepressor CoREST, histone demethlyase LSD1, HDAC1, HDAC2, BRAF35, and PHF21A. Esco2 also interacts with various histone methyltransferases Suv39h1, SETDB1 and G9a. Esco2 complex purified from HeLa nuclear extract possesses histone H3 K9 methylation activity and functions as a transcription repressor. Esco2 fused to Gal4 DNA binding domain represses transcription by increasing methylation of histone H3 K9 in the promoter region. These results suggest a novel function of Esco2 in transcription repression through modulation of the chromatin structure. (C) 2008 Elsevier Inc. All rights reserved.
引用
收藏
页码:298 / 304
页数:7
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