TY - JOUR
T1 - MBP-1 physically associates with histone deacetylase for transcriptional repression
AU - Ghosh, Asish K.
AU - Steele, Robert
AU - Ray, Ratna B.
N1 - Funding Information:
We thank D. Ayer, D. Dean, R. Eisenman, R. Evans, S. Schreiber, and Y. Shi for providing research materials. This research work was supported by PHS Grant CA-52799 from the National Cancer Institute.
PY - 1999/7/5
Y1 - 1999/7/5
N2 - 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.
AB - 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.
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U2 - 10.1006/bbrc.1999.0921
DO - 10.1006/bbrc.1999.0921
M3 - Article
C2 - 10403782
AN - SCOPUS:0033526809
SN - 0006-291X
VL - 260
SP - 405
EP - 409
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 2
ER -