MyoD recruits the cdk9/cyclin T2 complex on Myogenic-genes regulatory regions

Authors

  • Cristina Giacinti,

    1. Department of Biology, Sbarro Institute for Cancer Research and Molecular Medicine, College of Science and Technology Temple University, Philadelphia, Pennsylvania
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  • Luigi Bagella,

    1. Department of Biology, Sbarro Institute for Cancer Research and Molecular Medicine, College of Science and Technology Temple University, Philadelphia, Pennsylvania
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  • Pier Lorenzo Puri,

    1. DTI at Fondazione A. Cisalpino, ICBTE, San Raffaele Biomedical Science Park of Rome, Rome, Italy; The Burnham Institute, La Jolla, San Diego, California
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  • Antonio Giordano,

    Corresponding author
    1. Department of Biology, Sbarro Institute for Cancer Research and Molecular Medicine, College of Science and Technology Temple University, Philadelphia, Pennsylvania
    • Department of Biology, Sbarro Institute for Cancer Research and Molecular Medicine, College of Science and Technology Temple University, Philadelphia PA 19122.
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  • Cristiano Simone

    1. Department of Biology, Sbarro Institute for Cancer Research and Molecular Medicine, College of Science and Technology Temple University, Philadelphia, Pennsylvania
    2. Department of Biomedicine in Childhood, Division of Medical Genetics, University of Bari, Bari, Italy
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Abstract

During skeletal myogenesis, muscle-regulatory factors bHLH and MEF2 promote the expression of muscle-specific genes by recruiting several chromatin-modifying complexes on specific DNA regulatory sequences. A number of MyoD-interacting proteins have been reported, but whether they are recruited to the chromatin of myogenic loci, and the relationship with other chromatin bound proteins is unknown. We show that MyoD recruits cdk9/cyclin T2, together with the histone acetyltransferases p300 and PCAF, and the chromatin remodeling complex SWI/SNF, on promoters and enhancers of muscle-specific genes, and that this event correlates with the acetylation of histone tails, remodeling of chromatin, and phosphorylation of the C-terminal domain (CTD) of the RNA polymerase II at these elements. J.Cell.Physiol. © 2005 Wiley-Liss, Inc.

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