Kazuhiro Kataoka

The University of Tokyo, Tōkyō, Japan

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Publications (4)12.5 Total impact

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    ABSTRACT: The structural relationships between histone-binding proteins and DNA-binding proteins are important, since nucleosome-interacting factors possess histone-binding and/or DNA-binding components. S. cerevisiae (Sc) Cia1p/Asf1p, a homologue of human CIA (CCG1-interacting factor A), is the most evolutionarily conserved histone chaperone, which facilitates nucleosome assembly by interacting with the nucleosome entry site of the core histones H3/H4. The crystal structure of the evolutionarily conserved domain (residues 1-169) of Cia1p (ScCia1p-DeltaC2) was determined at 2.95 A resolution. The refined model contains 166 residues in the asymmetric unit. The overall tertiary structure resembles a beta-sandwich fold, and belongs to the "switched" immunoglobulin class of proteins. The crystal structure suggests that ScCia1p-DeltaC2 is structurally related to the DNA-binding proteins, such as NF-kappaB and its family members. This is the first examination of the structural similarities between a histone chaperone and DNA-binding proteins. We discuss the possibilities that the strands beta3 and beta4, which possess highly electronegative surface potentials, are the important regions for the interaction with core histones, and that the histone chaperone ScCia1p/Asf1p and the DNA-binding protein NF-kappaB may have evolved from the same prototypal protein class.
    No preview · Article · Jan 2006 · Journal of Biochemistry
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    ABSTRACT: The oncoprotein gankyrin plays a central role in tumorigenesis and cell proliferation. Gankyrin interacts with the retinoblastoma tumor suppressor (Rb) and cyclin-dependent kinase 4/6 (CDK4/6), increases phosphorylation at specific residues of Rb by CDK4/6 in vivo, and promotes tumorigenesis. The phosphorylation of Rb by CDK4/6 leads to the deregulation of the cell cycle during G1/S transition. Although how phosphorylation occurs on Rb has been studied extensively, the mechanism of site-specific phosphorylation of Rb remains unclear due to a lack of information on the structural arrangement of Rb and CDK4/6. Here, we have determined and refined to 2.3-A resolution the crystal structure of a gankyrin homolog, the non-ATPase subunit 6 (Nas6p) of the proteasome from yeast. The crystal structure reveals that Nas6p contains seven ankyrin repeats. The number of the repeats is different from that predicted from the primary structure. Nas6p also possesses an unusual curved structure with two acidic regions at the N- and C-terminal regions separated by one basic region, suggesting that it has at least two functional surfaces. The tertiary structure of Nas6p, together with the previous biochemical studies, indicates that the CDK4/6 and Rb binding surfaces of gankyrin are located at the N- and C-terminal regions, respectively, and face the same side of gankyrin. These observations suggest that gankyrin brings Rb and CDK4/6 together through gankyrin-Rb and gankyrin-CDK4/6 interactions and determines the relative positioning of the substrate (Rb) and the enzyme (CDK4/6). Our findings provide mechanistic insight into site-specific phosphorylation of Rb caused by CDK4/6.
    Preview · Article · Feb 2004 · Journal of Biological Chemistry
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    ABSTRACT: Yeast Cia1p is a homologue of human CIA (CCG1-interacting factor A), which possesses nucleosome-assembly activity and interacts with the human TFIID subunit CCG1 and the C-terminal domain of histone H3. The yeast Cia1p without the C-terminal polyanionic stretch has been expressed in Escherichia coli, purified to homogeneity and crystallized by the hanging-drop vapour-diffusion method using PEG 8000 as precipitant. The protein was crystallized in orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 106.70, b = 46.92, c = 40.60 A and one molecule in the asymmetric unit. The crystal diffracted beyond 2.95 A resolution using synchrotron radiation.
    No preview · Article · Nov 2002 · Acta Crystallographica Section D Biological Crystallography
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    ABSTRACT: The regulatory particle non-ATPase subunit, Nas6p, from Saccharomyces cerevisiae has been crystallized by the hanging-drop vapour-diffusion method using PEG 4000 as precipitant. The crystals belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 41.43 (2), b = 61.74 (1), c = 98.09 (2) A, and contain one molecule in the asymmetric unit. A complete diffraction data set using synchrotron radiation was collected to 2.6 A resolution.
    No preview · Article · Jun 2002 · Acta Crystallographica Section D Biological Crystallography