Open AccessInteraction and functional collaboration of p300/CBP and bHLH proteins in muscle and B-cell differentiation.
Author(s) -
Richard Eckner,
TsoPang Yao,
Elizabeth Oldread,
David M. Livingston
Publication year - 1996
Publication title -
genes and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.136
H-Index - 438
eISSN - 1549-5477
pISSN - 0890-9369
DOI - 10.1101/gad.10.19.2478
Subject(s) - biology , transcription factor , cellular differentiation , microbiology and biotechnology , fusion protein , basic helix loop helix , transcription (linguistics) , dna binding protein , lim domain , gene , genetics , recombinant dna , linguistics , philosophy , zinc finger
Differentiation of skeletal muscle cells and B lymphocytes is regulated by basic helix-loop-helix (bHLH) proteins. Both differentiation programs are inhibited by the adenovirus E1A oncoprotein. Analysis of E1A mutants has implicated two of its cellular-binding proteins, p300 and CBP, in controlling certain aspects of differentiation. We find that p300 can cooperate with tissue-specific bHLH proteins in activating target genes and requires only the bHLH domain of such proteins to stimulate E box-directed transcription. Importantly, the ability of bHLH proteins to activate transcription correlates with the presence of p300/CBP in E box-dependent DNA-binding complexes, because both phenomena require at least two adjacent E-box motifs. Microinjection of p300/CBP antibodies into myoblasts blocks terminal differentiation, cell fusion, and transcriptional activity of myogenic bHLH proteins. These results suggest that the function of p300/CBP is essential for the execution of key aspects of cellular differentiation.