A putative nuclear receptor coactivator (TMF/ARA160) associates with hbrm/hSNF2α and BRG-1/hSNF2β and localizes in the Golgi apparatus

An ATP-dependent chromatin remodeling factor, SNF/SWI complex, acts as a coactivator for numerous transcriptional factors. One of the best-documented examples is nuclear receptors, although the molecular mechanism for this coactivation has not been sufficiently elucidated. Here we show that hbrm/hSNF2alpha and BRG-1/hSNF2beta, the ATPase subunits of the human SNF/SWI complexes, specifically associate in vitro and in vivo with TATA element modulatory factor (TMF)/ ARA160, which has been described as a binding protein to and coactivator for the androgen receptor. This interaction requires highly conserved N-terminal regions of hbrm/hSNF2alpha and BRG-1/hSNF2beta and a C-terminal region of TMF/ARA160. Immunofluorescence and Western blot studies revealed that the TMF isoforms differentially localize in the Golgi apparatus and the nucleus. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.