TY - JOUR
T1 - Mechanism of c-Myb-C/EBPβ cooperation from separated sites on a promoter
AU - Tahirov, Tahir H.
AU - Sato, Ko
AU - Ichikawa-Iwata, Emi
AU - Sasaki, Motoko
AU - Inoue-Bungo, Taiko
AU - Shiina, Masaaki
AU - Kimura, Kazumi
AU - Takata, Shioka
AU - Fujikawa, Atsushi
AU - Morii, Hisayuki
AU - Kumasaka, Takashi
AU - Yamamoto, Masaki
AU - Ishii, Shunsuke
AU - Ogata, Kazuhiro
N1 - Funding Information:
We thank S. Akira for NF-IL6 cDNA, K. Takeyasu and A. Sarai for helpful comments, and M. Sato, N. Kamiya, T. Kato, I. Aoki, and M. Hosaka for generous support. AFM images were measured by T. Okada and R. Hirota of the Research Institute of Biomolecule Metrology, Tsukuba, Ibaraki, Japan. This research was in part supported by CREST (Core Research for Evolutional Science and Technology) of the Japan Science and Technology Corporation (JST) to K.O.
PY - 2002/1/11
Y1 - 2002/1/11
N2 - c-Myb, but not avian myeloblastosis virus (AMV) v-Myb, cooperates with C/EBPβ to regulate transcription of myeloid-specific genes. To assess the structural basis for that difference, we determined the crystal structures of complexes comprised of the c-Myb or AMV v-Myb DNA-binding domain (DBD), the C/EBPβ DBD, and a promoter DNA fragment. Within the c-Myb complex, a DNA-bound C/EBPβ interacts with R2 of c-Myb bound to a different DNA fragment; point mutations in v-Myb R2 eliminate such interaction within the v-Myb complex. GST pull-down assays, luciferase trans-activation assays, and atomic force microscopy confirmed that the interaction of c-Myb and C/EBPβ observed in crystal mimics their long range interaction on the promoter, which is accompanied by intervening DNA looping.
AB - c-Myb, but not avian myeloblastosis virus (AMV) v-Myb, cooperates with C/EBPβ to regulate transcription of myeloid-specific genes. To assess the structural basis for that difference, we determined the crystal structures of complexes comprised of the c-Myb or AMV v-Myb DNA-binding domain (DBD), the C/EBPβ DBD, and a promoter DNA fragment. Within the c-Myb complex, a DNA-bound C/EBPβ interacts with R2 of c-Myb bound to a different DNA fragment; point mutations in v-Myb R2 eliminate such interaction within the v-Myb complex. GST pull-down assays, luciferase trans-activation assays, and atomic force microscopy confirmed that the interaction of c-Myb and C/EBPβ observed in crystal mimics their long range interaction on the promoter, which is accompanied by intervening DNA looping.
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U2 - 10.1016/S0092-8674(01)00636-5
DO - 10.1016/S0092-8674(01)00636-5
M3 - Article
C2 - 11792321
AN - SCOPUS:18244394860
VL - 108
SP - 57
EP - 70
JO - Cell
JF - Cell
SN - 0092-8674
IS - 1
ER -