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A putative nuclear receptor coactivator (TMF/ARA160) associates with hbrm/hSNF2α and BRG‐1/hSNF2β and localizes in the Golgi apparatus
Author(s) -
Mori Katsuhiro,
Kato Hiroyuki
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02803-x
Subject(s) - coactivator , swi/snf , nuclear receptor coactivator 2 , nuclear receptor coactivator 1 , microbiology and biotechnology , nuclear receptor coactivator 3 , golgi apparatus , biology , cytoplasm , nuclear export signal , inner membrane , nuclear localization sequence , nuclear receptor , chromatin remodeling , cell nucleus , chromatin , transcription factor , endoplasmic reticulum , genetics , gene , mitochondrion
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/hSNF2α and BRG‐1/hSNF2β, 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/hSNF2α and BRG‐1/hSNF2β 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.