MBP-1 physically associates with histone deacetylase for transcriptional repression

Asish K. Ghosh, Robert Steele, Ratna B. Ray

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

MBP-1, a c-myc promoter binding protein, is a mammalian transcription factor with intriguing properties including transcriptional repression of cellular genes. Recently, we have identified and characterized two different repressor domains of MBP-1. In this report, we have demonstrated that MBP-1 physically associates with histone deacetylase (HDAC), thus promoting formation of neucleosomes that inhibit transcription. Trichostatin A, an inhibitor of histone deacetylase, significantly reduces MBP-1-mediated transcriptional repression. However, MBP-1-mediated repression on c-myc promoter is resistant to histone deacetylase activity. Our results suggest that MBP-1 represses transcription by recruiting histone deacetylase as one of the mechanisms, whereas the other mechanism is resistant to HDAC activity and probably related to direct binding of promoter sequences or interaction through yet unidentified factor.

Original languageEnglish (US)
Pages (from-to)405-409
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume260
Issue number2
DOIs
StatePublished - Jul 5 1999
Externally publishedYes

Fingerprint

Histone Deacetylases
Transcription
trichostatin A
Histone Deacetylase Inhibitors
Carrier Proteins
Transcription Factors
Genes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

MBP-1 physically associates with histone deacetylase for transcriptional repression. / Ghosh, Asish K.; Steele, Robert; Ray, Ratna B.

In: Biochemical and Biophysical Research Communications, Vol. 260, No. 2, 05.07.1999, p. 405-409.

Research output: Contribution to journalArticle

Ghosh, Asish K. ; Steele, Robert ; Ray, Ratna B. / MBP-1 physically associates with histone deacetylase for transcriptional repression. In: Biochemical and Biophysical Research Communications. 1999 ; Vol. 260, No. 2. pp. 405-409.
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