Activation function 1 domain plays a negative role in dimerization of estrogen receptor beta.
Transcriptional potential of estrogen receptor beta (ERbeta) depends on the ligand binding and subsequent dimerization of the receptor protein. In order to examine the role of N-terminally located activation function 1 (AF-1) protein domain in the dimerization process of ERbeta, we used yeast SOS-Recruitment System (SRS). Two variants of ERbeta protein were expressed in the yeast cells: full length receptor and a truncated form, lacking AF-1. We observed that upon 17beta-estradiol treatment only the shorter form of the receptor dimerized, whereas the full-length one did not. This result suggests an inhibitory function of AF-1 in dimer formation and supports previous studies showing that N-terminal domain of ERbeta suppresses transcriptional activity.
Detka
Daniel
D
Laboratory of Molecular Neurobiology, Nencki Institute of Experimental Biology, Pasteura 3, Warsaw 02-093, Poland.
Kalita
Katarzyna
K
Kaczmarek
Leszek
L
D049109:Cell Proliferation / Q000187:drug effects; D019281:Dimerization; D004958:Estradiol / Q000494:pharmacology; D047629:Estrogen Receptor beta / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D009154:Mutation / Q000235:genetics; D017434:Protein Structure, Tertiary / Q000235:genetics / Q000502:physiology; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000235:genetics / Q000378:metabolism; D020664:Son of Sevenless Proteins / Q000235:genetics
D047629:Estrogen Receptor beta; D011993:Recombinant Fusion Proteins; D020664:Son of Sevenless Proteins; D004958:Estradiol