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

Beom Jun Kim, Kyung Min Kang, Sung Yun Jung, Hyun Kyung Choi, Jong Hun Seo, Ji Hye Chae, Eun Jung Cho, Hong-Duk Youn, Jun Qin, Seong Tae Kim

Research output: Contribution to journalArticleResearchpeer-review

21 Citations (Scopus)

Abstract

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 acetyltransferase 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.

Original languageEnglish
Pages (from-to)298-304
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume372
Issue number2
DOIs
StatePublished - 25 Jul 2008

Fingerprint

Co-Repressor Proteins
Chromatids
Transcription
Histones
Chromatin
Methylation
Enzymes
Chromosome Segregation
Anaphase
Acetyltransferases
S Phase
Genetic Promoter Regions
Cell Division
Chromosomes
DNA
Cells
Modulation
Proteins

Keywords

  • CoREST
  • Cohesion
  • Esco2
  • LSD1
  • Methylation

Cite this

Kim, B. J., Kang, K. M., Jung, S. Y., Choi, H. K., Seo, J. H., Chae, J. H., ... Kim, S. T. (2008). Esco2 is a novel corepressor that associates with various chromatin modifying enzymes. Biochemical and Biophysical Research Communications, 372(2), 298-304. https://doi.org/10.1016/j.bbrc.2008.05.056
Kim, Beom Jun ; Kang, Kyung Min ; Jung, Sung Yun ; Choi, Hyun Kyung ; Seo, Jong Hun ; Chae, Ji Hye ; Cho, Eun Jung ; Youn, Hong-Duk ; Qin, Jun ; Kim, Seong Tae. / Esco2 is a novel corepressor that associates with various chromatin modifying enzymes. In: Biochemical and Biophysical Research Communications. 2008 ; Vol. 372, No. 2. pp. 298-304.
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abstract = "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 acetyltransferase 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.",
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Kim, BJ, Kang, KM, Jung, SY, Choi, HK, Seo, JH, Chae, JH, Cho, EJ, Youn, H-D, Qin, J & Kim, ST 2008, 'Esco2 is a novel corepressor that associates with various chromatin modifying enzymes', Biochemical and Biophysical Research Communications, vol. 372, no. 2, pp. 298-304. https://doi.org/10.1016/j.bbrc.2008.05.056

Esco2 is a novel corepressor that associates with various chromatin modifying enzymes. / Kim, Beom Jun; Kang, Kyung Min; Jung, Sung Yun; Choi, Hyun Kyung; Seo, Jong Hun; Chae, Ji Hye; Cho, Eun Jung; Youn, Hong-Duk; Qin, Jun; Kim, Seong Tae.

In: Biochemical and Biophysical Research Communications, Vol. 372, No. 2, 25.07.2008, p. 298-304.

Research output: Contribution to journalArticleResearchpeer-review

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