記述言語：英語   掲載種別：研究論文（学術雑誌）  

It is characteristic of eukaryotic transcription that a unique combination of multiple transcriptional regulatory proteins bound to promoter DNA specifically activate or repress downstream target genes; this is referred to as combinatorial gene regulation. Recently determined structures have revealed different modes of protein-protein interaction on the promoter DNA from near (e.g. the Runx1-CBFbeta-DNA, NFAT-Fos-Jun-DNA, GABPalpha-GABPbeta-DNA, Ets-1-Pax-5-DNA and PU.1-IRF-4-DNA complexes) and afar with DNA looping (e.g. the c-Myb-C/EBPbeta-DNA complex), and their regulatory mechanisms.

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記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1016/S0092-8674(01)00636-5

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記述言語：英語   掲載種別：研究論文（学術雑誌）  

c-Myb and the C/EBP family are transcriptional regulatory factors that act in concert to regulate the expression of myeloid-specific genes. v-Myb encoded by avian myeloblastosis virus (AMV) is a mutated form of c-Myb that contains point mutations which disrupt the cooperation with C/EBPs. To understand the mechanism of the transcriptional synergy between c-Myb and C/EBPs and the effect of the v-Myb mutations on that synergy, knowledge based on their three-dimensional structures is essential. Crystals of ternary complexes, in which various combinations of the DNA-binding domains of c-Myb or v-Myb and C/EBPalpha or C/EBPbeta are bound to a DNA fragment from tom-1A promoter, were obtained by the vapour-diffusion method. Complete diffraction data sets were obtained from each native crystal and two types of iodine-derivative crystals. A three-wavelength MAD data set was also obtained from a bromine-derivative crystal.

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記述言語：英語   掲載種別：研究論文（学術雑誌）  

The C-terminal fragment (residues 259-345) of human C/EBPbeta, a basic region leucine zipper transcriptional regulatory factor which includes the minimal DNA-binding domain, was crystallized in complex with a 16 bp DNA fragment from the tom-1 promoter. The crystals were in the form of a parallelepiped belonging to space group C222(1), had unit-cell parameters a = 100.7 (2), b = 113.5 (1), c = 74.4 (1) A and diffracted to a resolution of 2.1 A. Moreover, truncation of nine residues from the C-terminus not conserved among C/EBP family members yielded isomorphous crystals that diffracted to a resolution of 1.8 A or better. Truncation of 14 residues from the N-terminus of the C-terminal fragment produced well shaped crystals in the form of hexagonal bipyramids, however; unfortunately, they were unstable and diffracted poorly.

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記述言語：英語   掲載種別：研究論文（学術雑誌）  

Three types of protein-DNA complexes, AML1/Runx-1/CBFalpha(Runt)-CBFbeta-C/EBPbeta(bZip)-DNA (CBFalpha-beta-C/EBPbeta-DNA), AML1/Runx-1/CBFalpha(Runt)-C/EBPbeta(bZip)-DNA (CBFalpha-C/EBPbeta-DNA) and AML1/Runx-1/CBFalpha(Runt)-DNA (CBFalpha-DNA), were crystallized. The crystals were all orthorhombic and belonged to space groups C222(1), P2(1)2(1)2 and P2(1)2(1)2(1), respectively. The resolutions of CBFalpha-beta-C/EBPbeta-DNA and CBFalpha-C/EBPbeta-DNA crystals were both 3 A, while that of the CBFalpha-DNA crystal was 2.65 A. Complete data sets were collected for all of the native crystals, along with MAD and MIR data sets for CBFalpha-beta-C/EBPbeta-DNA. The heavy-atom site was determined using MAD data for a gold derivative of CBFalpha-beta-C/EBPbeta-DNA.

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記述言語：英語  

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記述言語：英語   掲載種別：研究論文（学術雑誌）  

DOI： 10.1016/S0092-8674(01)00271-9

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