Tomoko Mase
The University of Tokyo, Tokyo, Tokyo-to, Japan

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Publications (2)1.01 Total impact

  • Article: Structure of flap endonuclease 1 from the hyperthermophilic archaeon Desulfurococcus amylolyticus.
    Tomoko Mase, Keiko Kubota, Ken-ichi Miyazono, Yutaka Kawarabayasi, Masaru Tanokura
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    ABSTRACT: Flap endonuclease 1 (FEN1) is a key enzyme in DNA repair and DNA replication. It is a structure-specific nuclease that removes 5'-overhanging flaps and the RNA/DNA primer during maturation of the Okazaki fragment. Homologues of FEN1 exist in a wide range of bacteria, archaea and eukaryotes. In order to further understand the structural basis of the DNA recognition, binding and cleavage mechanism of FEN1, the structure of FEN1 from the hyperthermophilic archaeon Desulfurococcus amylolyticus (DaFEN1) was determined at 2.00 Å resolution. The overall fold of DaFEN1 was similar to those of other archaeal FEN1 proteins; however, the helical clamp and the flexible loop exhibited a putative substrate-binding pocket with a unique conformation.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 02/2011; 67(Pt 2):209-13. · 0.51 Impact Factor
  • Article: Crystallization and preliminary X-ray analysis of flap endonuclease 1 (FEN1) from Desulfurococcus amylolyticus.
    Tomoko Mase, Keiko Kubota, Ken-ichi Miyazono, Yutaka Kawarabayasi, Masaru Tanokura
    [show abstract] [hide abstract]
    ABSTRACT: Flap endonuclease 1 (FEN1) is a structure-specific nuclease that removes 5'-overhanging flaps in DNA repair and removes the RNA/DNA primer during maturation of the Okazaki fragment in lagging-strand DNA replication. FEN1 from the hyperthermophilic archaeon Desulfurococcus amylolyticus was expressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method with monoammonium dihydrogen phosphate as the precipitant at pH 8.3. X-ray diffraction data were collected to 2.00 A resolution. The space group of the crystal was determined as the primitive hexagonal space group P321, with unit-cell parameters a = b = 103.76, c = 84.58 A. The crystal contained one molecule in the asymmetric unit.
    Acta Crystallographica Section F Structural Biology and Crystallization Communications 10/2009; 65(Pt 9):923-5. · 0.51 Impact Factor

Institutions

  • 2009–2011
    • The University of Tokyo
      • Department of Applied Biological Chemistry
      Tokyo, Tokyo-to, Japan
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