Identification of a novel BRMS1-homologue protein p40 as a component of the mSin3A/p33 ING1b/HDAC1 deacetylase complex

Anatoly Y. Nikolaev, Nikolaos A. Papanikolaou, Muyang Li, Jun Qin, Wei Gu

Research output: Contribution to journalArticlepeer-review

Abstract

Repression of gene transcription is mediated by histone deacetylases containing repressor-co-repressor complexes, which are recruited to promoters of target genes via interactions with sequence-specific transcription factors. The mammalian Sin3A co-repressor complex contains a core of at least seven proteins including the pRb-interacting protein RBP1 and a putative tumor suppressor p33 ING1b. By biochemical purification and mass spectrometry, we have identified a novel component p40 from this complex. p40 bears homology to both yeast Sds3, a component of yeast histone deacetylase complexes, and its mammalian homologue mSds3. The p40-associated complex purified from human cells shows a strong histone deacetylase activity. When tethered to a Gal-DNA binding domain, the Gal-p40 is able to significantly repress transcription of a Gal-luciferase promoter. Interestingly, database analysis reveals that p40 is also highly homologous to BRMS1, a breast carcinoma metastasis suppressor, and overexpression of p40 in human cells can significantly inhibit cell growth. Thus, our data indicate that p40 may be critically involved in transcription repression of cell growth-associated gene expression by recruiting the HDAC1 deacetylase complex.

Original languageEnglish (US)
Pages (from-to)1216-1222
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume323
Issue number4
DOIs
StatePublished - Oct 29 2004
Externally publishedYes

Keywords

  • Breast carcinoma
  • BRMS1
  • Growth repression
  • Histone deacetylase
  • p33
  • Sin3A
  • Transcriptional co-repressor
  • Tumor suppressor

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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