Identity between TRAP and SMCC complexes indicates novel pathways for the function of nuclear receptors and diverse mammalian activators.

The human thyroid hormone receptor-associated protein (TRAP) complex, an earlier described coactivator for nuclear receptors, and an SRB- and MED-containing cofactor complex (SMCC) that mediates activation by Gal4-p53 are shown to be virtually the same with respect to specific polypeptide subunits, coactivator functions, and mechanisms of action (activator interactions). In ...
parallel with ligand-dependent interactions of nuclear receptors with the TRAP220 subunit, p53 and VP16 activation domains interact directly with a newly cloned TRAP80 subunit. These results indicate novel pathways for the function of nuclear receptors and other activators (p53 and VP16) through a common coactivator complex that is likely to target RNA polymerase II. Identification of the TRAP230 subunit as a previously predicted gene product also suggests a coactivator-related transcription defect in certain disease states.
Mesh Terms:
Amino Acid Sequence, Blotting, Northern, Blotting, Western, Carrier Proteins, Cloning, Molecular, Fungal Proteins, Gene Expression Regulation, Hela Cells, Herpes Simplex Virus Protein Vmw65, Humans, Mediator Complex, Mediator Complex Subunit 1, Molecular Sequence Data, Protein Binding, RNA Polymerase II, Receptors, Calcitriol, Receptors, Thyroid Hormone, Response Elements, Saccharomyces cerevisiae Proteins, Trans-Activators, Transcription Factors, Tumor Suppressor Protein p53
Mol. Cell
Date: Mar. 01, 1999
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