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A novel Rb- and p300-binding protein inhibits transactivation by MyoD.

The retinoblastoma protein (Rb) regulates both the cell cycle and tissue-specific transcription, by modulating the activity of factors that associate with its A-B and C pockets. In skeletal muscle, Rb has been reported to regulate irreversible cell cycle exit and muscle-specific transcription. To identify factors interacting with Rb in muscle cells, we utilized the yeast two-hybrid system, using the A-B and C pockets of Rb as bait. A novel protein we have designated E1A-like inhibitor of differentiation 1 (EID-1), was the predominant Rb-binding clone isolated. It is preferentially expressed in adult cardiac and skeletal muscle and encodes a 187-amino-acid protein, with a classic Rb-binding motif (LXCXE) in its C terminus. Overexpression of EID-1 in skeletal muscle inhibited tissue-specific transcription. Repression of skeletal muscle-restricted genes was mediated by a block to transactivation by MyoD independent of G(1) exit and, surprisingly, was potentiated by a mutation that prevents EID-1 binding to Rb. Inhibition of MyoD may be explained by EID-1's ability to bind and inhibit p300's histone acetylase activity, an essential MyoD coactivator. Thus, EID-1 binds both Rb and p300 and is a novel repressor of MyoD function.

Pubmed ID: 11073990


  • MacLellan WR
  • Xiao G
  • Abdellatif M
  • Schneider MD


Molecular and cellular biology

Publication Data

December 19, 2000

Associated Grants

  • Agency: NHLBI NIH HHS, Id: K08 HL03671
  • Agency: NHLBI NIH HHS, Id: R01 HL47567
  • Agency: NHLBI NIH HHS, Id: R01 HL61668

Mesh Terms

  • Acetyltransferases
  • Adenovirus E1A Proteins
  • Amino Acid Sequence
  • Cloning, Molecular
  • Gene Expression Regulation
  • Histone Acetyltransferases
  • Molecular Sequence Data
  • Muscle, Skeletal
  • MyoD Protein
  • Nuclear Proteins
  • Protein Binding
  • Repressor Proteins
  • Retinoblastoma Protein
  • Saccharomyces cerevisiae Proteins
  • Tissue Distribution
  • Trans-Activators
  • Transcriptional Activation
  • Two-Hybrid System Techniques