Mechanism of c-Myb-C/EBPβ cooperation from separated sites on a promoter

Tahir H. Tahirov; Ko Sato; Emi Ichikawa-Iwata; Motoko Sasaki; Taiko Inoue-Bungo; Masaaki Shiina; Kazumi Kimura; Shioka Takata; Atsushi Fujikawa; Hisayuki Morii; Takashi Kumasaka; Masaki Yamamoto; Shunsuke Ishii; Kazuhiro Ogata

doi:10.1016/S0092-8674(01)00636-5

Mechanism of c-Myb-C/EBPβ cooperation from separated sites on a promoter

Tahir H. Tahirov, Ko Sato, Emi Ichikawa-Iwata, Motoko Sasaki, Taiko Inoue-Bungo, Masaaki Shiina, Kazumi Kimura, Shioka Takata, Atsushi Fujikawa, Hisayuki Morii, Takashi Kumasaka, Masaki Yamamoto, Shunsuke Ishii, Kazuhiro Ogata

Research output: Contribution to journal › Article › peer-review

129 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	57-70
Number of pages	14
Journal	Cell
Volume	108
Issue number	1
DOIs	https://doi.org/10.1016/S0092-8674(01)00636-5
State	Published - Jan 11 2002
Externally published	Yes

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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Mechanism of c-Myb-C/EBPβ cooperation from separated sites on a promoter. / Tahirov, Tahir H.; Sato, Ko; Ichikawa-Iwata, Emi; Sasaki, Motoko; Inoue-Bungo, Taiko; Shiina, Masaaki; Kimura, Kazumi; Takata, Shioka; Fujikawa, Atsushi; Morii, Hisayuki; Kumasaka, Takashi; Yamamoto, Masaki; Ishii, Shunsuke; Ogata, Kazuhiro.

In: Cell, Vol. 108, No. 1, 11.01.2002, p. 57-70.

Research output: Contribution to journal › Article › peer-review

Tahirov, Tahir H. ; Sato, Ko ; Ichikawa-Iwata, Emi ; Sasaki, Motoko ; Inoue-Bungo, Taiko ; Shiina, Masaaki ; Kimura, Kazumi ; Takata, Shioka ; Fujikawa, Atsushi ; Morii, Hisayuki ; Kumasaka, Takashi ; Yamamoto, Masaki ; Ishii, Shunsuke ; Ogata, Kazuhiro. / Mechanism of c-Myb-C/EBPβ cooperation from separated sites on a promoter. In: Cell. 2002 ; Vol. 108, No. 1. pp. 57-70.

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abstract = "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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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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