TY - JOUR
T1 - Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
AU - Chen, Hongwu
AU - Lin, Richard J.
AU - Schiltz, R. Louis
AU - Chakravarti, Debabrata
AU - Nash, Alyssa
AU - Nagy, Laszlo
AU - Privalsky, Martin L.
AU - Nakatani, Yoshihiro
AU - Evans, Ronald M.
N1 - Funding Information:
We acknowledge Dr. David No for Northern analysis and Henry Juguilon and Sheryl Moles for technical assistance. We are grateful to Dr. John Schwabe for critical reading of the manuscript. We thank Drs. M. Gstaiger and W. Schaffner for the gift of plasmids and yeast strain RH1533. R. J. L. is a predoctoral fellow of the Lucille P. Markey Charitable Trust. D. C. is a fellow of the Jane Coffin Childs Memorial Fund. R. M. E. is an Investigator of the Howard Hughes Medical Institute at the Salk Institute for Biological Studies. This work was supported by the Howard Hughes Medical Institute and National Institutes of Health grants GM26444 and HD27183.
PY - 1997/8/8
Y1 - 1997/8/8
N2 - We report here the identification of a novel cofactor, ACTR, that directly binds nuclear receptors and stimulates their transcriptional activities in a hormone-dependent fashion. ACTR also recruits two other nuclear factors, CBP and P/CAF, and thus plays a central role in creating a multisubunit coactivator complex. In addition, and unexpectedly, we show that purified ACTR is a potent histone acetyltransferase and appears to define a distinct evolutionary branch to this recently described family. Thus, hormonal activation by nuclear receptors involves the mutual recruitment of at least three classes of histone acetyltransferases that may act cooperatively as an enzymatic unit to reverse the effects of histone deacetylase shown to be part of the nuclear receptor corepressor complex.
AB - We report here the identification of a novel cofactor, ACTR, that directly binds nuclear receptors and stimulates their transcriptional activities in a hormone-dependent fashion. ACTR also recruits two other nuclear factors, CBP and P/CAF, and thus plays a central role in creating a multisubunit coactivator complex. In addition, and unexpectedly, we show that purified ACTR is a potent histone acetyltransferase and appears to define a distinct evolutionary branch to this recently described family. Thus, hormonal activation by nuclear receptors involves the mutual recruitment of at least three classes of histone acetyltransferases that may act cooperatively as an enzymatic unit to reverse the effects of histone deacetylase shown to be part of the nuclear receptor corepressor complex.
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U2 - 10.1016/S0092-8674(00)80516-4
DO - 10.1016/S0092-8674(00)80516-4
M3 - Article
C2 - 9267036
AN - SCOPUS:0030740253
SN - 0092-8674
VL - 90
SP - 569
EP - 580
JO - Cell
JF - Cell
IS - 3
ER -