From Wikipedia, the free encyclopedia


The mSin3 interaction domain (SID) is an interaction domain which is present on several transcriptional repressor proteins including TGFβ ( transforming growth factor β) and Mad. It interacts with the paired amphipathic alpha-helix 2 (PAH2) domain of mSin3, a transcriptional repressor domain that is attached to transcription repressor proteins such as the mSin3A corepressor.

Action of histone deacetylase 1 and 2 (HDAC1/2) is induced by the interaction of mSin3A with a multi-protein complex containing HDAC1/2. Transcription is also repressed by histone deacetylase-independent means.

External links

  • Wotton D, Knoepfler PS, Laherty CD, Eisenman RN, Massagué J (September 2001). "The Smad transcriptional corepressor TGIF recruits mSin3". Cell Growth Differ. 12 (9): 457–63. PMID  11571228.
  • A 13-Amino Acid Amphipathic α-Helix Is Required for the Functional Interaction between the Transcriptional Repressor Mad1 and mSin3A
  • Zhang JS, Moncrieffe MC, Kaczynski J, Ellenrieder V, Prendergast FG, Urrutia R (August 2001). "A conserved alpha-helical motif mediates the interaction of Sp1-like transcriptional repressors with the corepressor mSin3A". Mol. Cell. Biol. 21 (15): 5041–9. doi: 10.1128/MCB.21.15.5041-5049.2001. PMC  87230. PMID  11438660.


From Wikipedia, the free encyclopedia


The mSin3 interaction domain (SID) is an interaction domain which is present on several transcriptional repressor proteins including TGFβ ( transforming growth factor β) and Mad. It interacts with the paired amphipathic alpha-helix 2 (PAH2) domain of mSin3, a transcriptional repressor domain that is attached to transcription repressor proteins such as the mSin3A corepressor.

Action of histone deacetylase 1 and 2 (HDAC1/2) is induced by the interaction of mSin3A with a multi-protein complex containing HDAC1/2. Transcription is also repressed by histone deacetylase-independent means.

External links

  • Wotton D, Knoepfler PS, Laherty CD, Eisenman RN, Massagué J (September 2001). "The Smad transcriptional corepressor TGIF recruits mSin3". Cell Growth Differ. 12 (9): 457–63. PMID  11571228.
  • A 13-Amino Acid Amphipathic α-Helix Is Required for the Functional Interaction between the Transcriptional Repressor Mad1 and mSin3A
  • Zhang JS, Moncrieffe MC, Kaczynski J, Ellenrieder V, Prendergast FG, Urrutia R (August 2001). "A conserved alpha-helical motif mediates the interaction of Sp1-like transcriptional repressors with the corepressor mSin3A". Mol. Cell. Biol. 21 (15): 5041–9. doi: 10.1128/MCB.21.15.5041-5049.2001. PMC  87230. PMID  11438660.



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