Identification of the functional domains of ANT-1, a novel coactivator of the androgen receptor.
Previously, we identified a transcriptional coactivator for the activation function-1 (AF-1) domain of the human androgen receptor (AR) and designated it androgen receptor N-terminal domain transactivating protein-1 (ANT-1). This coactivator, which contains multiple tetratricopeptide repeat (TPR) motifs from amino acid (aa) 294, is identical to a component of U5 small nuclear ribonucleoprotein particles and binds specifically to the AR or glucocorticoid receptor. Here, we identified four distinct functional domains. The AR-AF-1-binding domain, which bound to either aa 180-360 or 360-532 in AR-AF-1, clearly overlapped with TAU-1 and TAU-5. This domain and the subnuclear speckle formation domain in ANT-1 were assigned within the TPR motifs, while the transactivating and nuclear localization signal domains resided within the N-terminal sequence. The existence of these functional domains may further support the idea that ANT-1 can function as an AR-AF-1-specific coactivator while mediating a transcription-splicing coupling.
Fan
Shuli
S
Department of Medicine and Bioregulatory Science (3rd Department of Internal Medicine), Graduate School of Medical Sciences, Kyushu University, Higashi-ku, Fukuoka, Japan.
Goto
Kiminobu
K
Chen
Guangchun
G
Morinaga
Hidetaka
H
Nomura
Masatoshi
M
Okabe
Taijiro
T
Nawata
Hajime
H
Yanase
Toshihiko
T
D033741:Adenine Nucleotide Translocator 1 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D019943:Amino Acid Substitution; D000818:Animals; D001665:Binding Sites; D019556:COS Cells; D002522:Chlorocebus aethiops; D051379:Mice; D016297:Mutagenesis, Site-Directed; D041681:NIH 3T3 Cells; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011944:Receptors, Androgen / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013347:Subcellular Fractions / Q000378:metabolism*
D033741:Adenine Nucleotide Translocator 1; D011944:Receptors, Androgen