OKI Masaya

FacultyApplied Chemistry and Biotechnology
Teacher OrganizationApplied Chemistry and Biotechnology
Education and
 Research Organization
Faculty of Engineering /Graduate School of Engineering
PositionProfessor
Last Updated: 19/10/15 22:24

Researcher Profile & Settings

Name

    OKI Masaya

Affiliation

  •  Applied Chemistry and Biotechnology Professor

Education

  • Apr. 1996Mar. 1999Kyushu University 分子生命科学系専攻
  • Apr. 1994Mar. 1996Toyama University 化学生物工学

Overseas travel history

  • アメリカ合衆国 米国立衛生研究所(NIH) Apr.  2001- Jun. 2005

Research Activities

Published Papers

  • Altered metabolic regulation owing to gsp1 mutations, encoding the nuclear small G protein in Saccharomyces cerevisiae.
    N.Hayashi and M.Oki
    Current Genetics 2019 Refereed
  • Histone H2A T120 Phosphorylation Promotes Oncogenic Transformation via Upregulation of Cyclin D1.
    Aihara H, Nakagawa T, Mizusaki H, Yoneda M, Kato M, Doiguchi M, Imamura Y, Higashi M, Ikura T, Hayashi T, Kodama Y, Oki M, Nakayama T, Cheung E, Aburatani H, Takayama KI, Koseki H, Inoue S, Takeshima Y, Ito T.
    Mol.Cell 64(1) 176-188 Oct.  2016 Refereed
  • Four domains of Ada1 form a heterochromatin boundary through different mechanisms.
    Kamata K, Shinmyozu K, Nakayama JI, Hatashita M, Uchida H, Oki M.
    Genes Cells. 21(10) 1125-1136 Oct.  2016 Refereed
  • Gic1 is a novel heterochromatin boundary protein in vivo.
    Mitsumori R, Shinmyozu K, Nakayama JI, Uchida H, Oki M.
    Genes Genet Syst. 91(3) 151-159 Nov.  2016 Refereed
  • Analysis of novel Sir3 binding regions in Saccharomyces cerevisiae.
    Mitsumori R, Ohashi T, Kazuto K, Ichino A, Kei Taniguchi, Kunihiro Ohta, Uchida H, Oki M
    J. Biochem. 160(1) 11-17 Jul.  2016 Refereed
  • Temperature-sensitive defects of the GSP1 gene, yeast Ran homologue, activate the Tel1-dependent pathway
    Naoyuki Hayashi, Seishi Murakami, Susumu Tsurusaki, Zen-ichiro Nagaura, Masaya Oki, Hideo Nishitani, Masahiko Kobayashi, Hiroko Shimizu, Ken-ichi Yamamoto, Takeharu Nishimoto
     353 330-336 2007 Refereed
  • Role of histone phosphorylation in chromatin dynamics and its implications in diseases
    Masaya Oki, Hitoshi Aihara, Takashi Ito
     41 319-336 2007 Refereed
  • Identification of novel suppressors for Mog1 implies its involvement in RNA metabolism, lipid metabolism and signal transduction
    Masaya Oki, Li Ma, Yonggang Wang, Akira Hatanaka, Chie Miyazato, Kazuo Tatebayashi, HIdeo Nishitani, HIroyuki Uchida, Takeharu Nishimoto
     400 114-121 2007 Refereed
  • H2A.Z functions to regulate progression through the cell cycle
    Namrita Dhillon, Masaya Oki, Shawn J. Szyjka, Oscar M. Aparicio, Rohinton T. Kamakaka
     26(2) 489-501 2006 Refereed
  • Different mating-type-regulated genes affect the DNA repair defects of Saccharomyces RAD51, RAD52 and RAD55 mutants
    Maria Valencia-Burton, Masaya Oki, Jean Johnson, Tracey A. Seier, Rohinton T. Kamakaka, James E. Haber
     174 41-55 2006 Refereed
  • Barrier function at HMR
    Masaya Oki, Rohinton T. Kamakaka
     197 707-716 Sep.  2005 Refereed
  • Analysis of barriers
    Masaya Oki
     Jan.  2005 Refereed
  • Analysis of HMR barriers
    Masaya Oki, Kamakaka RT
     Jul.  2004
  • Barrier proteins remodel and modify chromatin to restrict silenced domains
    Masaya Oki, Lourdes Valenzuela, Tomoko Chiba, Takashi Ito, Rohinton T. Kamakaka
     24(5) 1956-1967 2004 Refereed
  • Genome-wide analysis of heterochromatin barrier function in S.cerevisiae
    Masaya Oki, Chiba T, Ito t, Kamakaka RT
     Mar.  2003
  • Blockers and barriers to transcription : competing activities
    Masaya Oki, Rohinton T Kamakaka
     14 299-304 2002 Refereed
  • The Saccharomyces cerevisiae small GTPase, Gsp1p/Ran , is involved in 3' processing of 7S-to-5.8S rRNA and in degradation of the excised 5'-A0 fragment of 35S pre-rRNA, both of which are carried out by the exosome
    Nobuhiro Suzuki, Eishi Noguchi, Nobutaka Nakashima, Masaya Oki, Tomoyuki Ohba, Alan Tartakoff, Masamichi Ohishi, Takeharu Nishimoto
     158 613-625 Jun.  2001 Refereed
  • Mog1p stimulates a nucleotide release from GTP-Gsp1p which is inhibited by Yrb1p, but not from GDP-Gsp1p
    Masaya Oki, Nishimoto T
     Jul.  2000
  • Yrb1p interaction with the Gsp1p C terminus blocks Mog1p stimulation of GTP release from Gsp1p
    Masaya Oki, Takeharu Nishimoto
     275(42) 32894-32900 Jan.  2000 Refereed
  • A protein required for nuclear-protein import, Mog1p, directly interacts with GTP-Gsp1p, the Saccharomyces cerevisiae Ran homologue
    Masaya Oki, Takeharu Nishimoto
     95 15388-15393 Dec.  1998 Refereed
  • A novel protein required for nuclear protein import, Mog1p, directly interacts with GTP-bound Gsp1p, Saccharomyces cerevisiae Ran-homologe
    Masaya Oki, Nishimoto T
     Dec.  1998
  • Promoter/repressor system in Lactobacillus plantarum phage φg1e:characterization of the promoter pR49-pR-pL and overproduction of the cro-like protein Cng in Eschrichia coli.
    Makiko Kakikawa, Nobukatsu Watanabe, Tatsuya Funawatashi, Masaya Oki, Hiroo Yasukawa, Akira Taketo, Ken-Ichi Kodaira
     215 371-379 1998 Refereed
  • Nuclear protein import, but not mRNA export, is defective in all Saccharomyces cerevisiae mutants that produce temperature-sensitive forms of the Ran GTPase homologue Gsp1p
    Masaya Oki, Eishi Noguchi, Naoyuki Hayashi, Takeharu Nishimoto
     257 624-634 1998 Refereed
  • Nuclear protein import, but not mRNA export, is defective in all of the temperature sensitive mutants of the Saccharomyces cerevisiae Ran homologue Gsp1p GTPase
    Masaya Oki, Noguchi E, Hayashi N, Nishimoto T
     Nov.  1997
  • Characterization of the genes encoding integrative and excisive functions of Lactobacillus phage φg1e: clonig,sequence analysis, and expression in Escherishia coli
    Makiko Kakikawa, Masaya Oki, Nobukatsu Watanabe, Hiroo Yasukawa, Yukito Masamune, Akira Taketo, Ken-Ichi Kodaira
     185 119-125 1997 Refereed
  • Genome structure of the Lactobacillus temperate phage φg1e: the whole genome sequence and the putative promoter/repressor system
    Ken-Ichi Kodaira, Masaya Oki, Makiko Kakikawa, Nobukatsu Watanabe, Machiko Hirakawa, Kazuyo Yamada, Akira Taketo
     187 45-53 1997 Refereed
  • Functional and structural features of the holin HOL protein of the Lactobacillus plantarum phage φg1e: analysis in Escherishia coli system
    Masaya Oki, Makiko Kakikawa, Shogo Nakamura, Ei-Tora Yamamura, Kouichi Watanabe, Masae Sasamoto, Akira Taketo, Ken-Ichi Kodaira
     197 137-145 1997 Refereed
  • Cloning and nucleotido sequence of the major capsid protein of Lactobacillus bacteriophage φg1e
    Makiko Kakikawa, Masaya Oki, Hisayuki Tadokoro, Shogo Nakamura, Akira Taketo, Ken-Ichi Kodaira
     175 157-165 1996 Refereed
  • The virion proteins encoded by bacteriophage φK and its host-range mutant φKhT:host-range determination and DNA binding properties
    Ken-Ichi Kodaira, Masaya Oki, Makiko Kakikawa, Hisashi Kimoto, Akira Taketo
     119 1062-1069 1996 Refereed
  • Genome structure of a Lactobacillus plasmid pNMO belonging to the rolling-circle type replicon
    Masaya Oki, Makiko Kakikawa, Akira Taketo, Ken-Ichi Kodaira
     42 271-283 1996 Refereed
  • Cloning, sequence analysis, and expression of the genes encoding lytic functions of Lactobacillus bacteriophage φg1e
    Masaya Oki, Makiko Kakikawa, Kazuyo Yamada, Akira Taketo, Ken-Ichi Kodaira
     176 215-223 1996 Refereed
  • Determination of the single stranded origin of Shigella sonnei plasmid pKYM
    Ken-Ichi Kodaira, Masaya Oki, Akira Taketo, Hiroo Yasukawa, Yukito Masamune
     1260 183-190 1995 Refereed
  • The N-terminus and Tudor domains of Sgf29 are important for its heterochromatin boundary formation function
    Kamata, Kazuma;Goswami, Gayatri;Kashio, Sayaka;Urano, Takeshi;Nakagawa, Reiko;Uchida, Hiroyuki;Oki, Masaya
    JOURNAL OF BIOCHEMISTRY 155(3) 159-171 2014
  • 単一細胞の世代を越えたエピジェネティックな発現状態変化
    Newsletter of Japan Society for Comparative Endocrinology 40(151) 22-24 2014
  • 世代を越えたエピジェネティックな遺伝子発現変化の規則性:単一細胞追跡システムによって見えてきたもの
    OKI Masaya
    KAGAKU TO SEIBUTSU 52(9) 568-570 2014
  • Analysis of novel Sir3 binding regions in Saccharomyces cerevisiae.
    Mitsumori Risa;Ohashi Tomoe;Kugou Kazuto;Ichino Ayako;Taniguchi Kei;Ohta Kunihiro;Uchida Hiroyuki;Oki Masaya
    Journal of biochemistry 160(1) 2016
    :In Saccharomyces cerevisiae, the HMR, HML, telomere and rDNA regions are silenced. Silencing at the rDNA region requires Sir2, and silencing at the HMR, HML and telomere regions requires binding of a protein complex, consisting of Sir2, Sir3 and Sir4, that mediates repression of gene expression. Here, several novel Sir3 binding domains, termed CN domains (Chromosomal Novel Sir3 binding region), were identified using chromatin immunoprecipitation (ChIP) on chip analysis of S. cerevisiae chromosomes. Furthermore, analysis of G1-arrested cells demonstrated that Sir3 binding was elevated in G1-arrested cells compared with logarithmically growing asynchronous cells, and that Sir3 binding varied with the cell cycle. In addition to 14 CN regions identified from analysis of logarithmically growing asynchronous cells (CN1-14), 11 CN regions were identified from G1-arrested cells (CN15-25). Gene expression at some CN regions did not differ between WT and sir3Δ strains. Sir3 at conventional heterochromatic regions is thought to be recruited to chromosomes by Sir2 and Sir4; however, in this study, Sir3 binding occurred at some CN regions even in sir2Δ and sir4Δ backgrounds. Taken together, our results suggest that Sir3 exhibits novel binding parameters and gene regulatory functions at the CN binding domains.
  • Gic1 is a novel heterochromatin boundary protein in vivo.
    Mitsumori Risa;Shinmyozu Kaori;Nakayama Jun-Ichi;Uchida Hiroyuki;Oki Masaya
    Genes & genetic systems 91(3) 2016
    :In Saccharomyces cerevisiae, HMR/HML, telomeres and ribosomal DNA are heterochromatin-like regions in which gene transcription is prevented by the silent information regulator (Sir) complex. The Sir complex (Sir2, Sir3 and Sir4) can spread through chromatin from the silencer. Boundaries prevent Sir complex spreading, and we previously identified 55 boundary genes among all ~6,000 yeast genes. These boundary proteins can be distinguished into two types: those that activate transcription to prevent spreading of silencing, and those that prevent gene silencing by forming a boundary. We selected 44 transcription-independent boundary proteins from the 55 boundary genes by performing a one-hybrid assay and focused on GIC1 (GTPase interaction component 1). Gic1 is an effector of Cdc42, which belongs to the Rho family of small GTPases, and has not been reported to function in heterochromatin boundaries in vivo. We detected a novel boundary-forming activity of Gic1 at HMR-left and telomeric regions by conducting a chromatin immunoprecipitation assay with an anti-Sir3 antibody. We also found that Gic1 bound weakly to histones in two-hybrid analysis. Moreover, we performed domain analysis to identify domain(s) of Gic1 that are important for its boundary activity, and identified two minimum domains, which are located outside its Cdc42-binding domain.
  • Four domains of Ada1 form a heterochromatin boundary through different mechanisms.
    Kamata Kazuma;Shinmyozu Kaori;Nakayama Jun-Ichi;Hatashita Masanori;Uchida Hiroyuki;Oki Masaya
    Genes to cells : devoted to molecular & cellular mechanisms 21(10) 2016
    :In eukaryotic cells, there are two chromatin states, silenced and active, and the formation of a so-called boundary plays a critical role in demarcating these regions; however, the mechanisms underlying boundary formation are not well understood. In this study, we focused on S. cerevisiae ADA1, a gene previously shown to encode a protein with a robust boundary function. Ada1 is a component of the histone modification complex Spt-Ada-Gcn5-acetyltransferase (SAGA) and the SAGA-like (SLIK) complex, and it helps to maintain the integrity of these complexes. Domain analysis showed that four relatively small regions of Ada1 (Region I; 66-75 aa, II; 232-282 aa, III; 416-436 aa and IV; 476-488 aa) have a boundary function. Among these, Region II could form an intact SAGA complex, whereas the other regions could not. Investigation of cellular factors that interact with these small regions identified a number of proteasome-associated proteins. Interestingly, the boundary functions of Region II and Region III were affected by depletion of Ump1, a maturation and assembly factor of the 20S proteasome. These results suggest that the boundary function of Ada1 is functionally linked to proteasome processes and that the four relatively small regions in ADA1 form a boundary via different mechanisms.
  • Gic1 is a novel heterochromatin boundary protein in vivo
    Mitsumori Risa;Shinmyozu Kaori;Nakayama Jun-ichi;Uchida Hiroyuki;Oki Masaya
    Genes & Genetic Systems 91(3) 151-159 2016

    In Saccharomyces cerevisiae, HMR/HML, telomeres and ribosomal DNA are heterochromatin-like regions in which gene transcription is prevented by the silent information regulator (Sir) complex. The Sir complex (Sir2, Sir3 and Sir4) can spread through chromatin from the silencer. Boundaries prevent Sir complex spreading, and we previously identified 55 boundary genes among all ~6,000 yeast genes. These boundary proteins can be distinguished into two types: those that activate transcription to prevent spreading of silencing, and those that prevent gene silencing by forming a boundary. We selected 44 transcription-independent boundary proteins from the 55 boundary genes by performing a one-hybrid assay and focused on GIC1 (GTPase interaction component 1). Gic1 is an effector of Cdc42, which belongs to the Rho family of small GTPases, and has not been reported to function in heterochromatin boundaries in vivo. We detected a novel boundary-forming activity of Gic1 at HMR-left and telomeric regions by conducting a chromatin immunoprecipitation assay with an anti-Sir3 antibody. We also found that Gic1 bound weakly to histones in two-hybrid analysis. Moreover, we performed domain analysis to identify domain(s) of Gic1 that are important for its boundary activity, and identified two minimum domains, which are located outside its Cdc42-binding domain.

  • tRNA Genes Affect Chromosome Structure and Function via Local Effects
    Hamdani, Omar;Dhillon, Namrita;Hsieh, Tsung-Han S.;Fujita, Takahiro;Ocampo, Josefina;Kirkland, Jacob G.;Lawrimore, Josh;Kobayashi, Tetsuya J.;Friedman, Brandon;Fulton, Derek;Wu, Kenneth Y.;Chereji, Rzvan, V;Oki, Masaya;Bloom, Kerry;Clark, David J.;Rando, Oliver J.;Kamakaka, Rohinton T.
    MOLECULAR AND CELLULAR BIOLOGY 39(8) Apr.  2019 Refereed
  • The microenvironment surrounding FAD mediates its conversion to 8-formyl-FAD in Aspergillus oryzae RIB40 formate oxidase.
    Doubayashi Daiju;Oki Masaya;Mikami Bunzo;Uchida Hiroyuki
    Journal of biochemistry 2019 Refereed
    :Aspergillus oryzae RIB40 formate oxidase has Arg87 and Arg554 near the formyl group and O(4) atom of 8-formyl-flavin adenine dinucleotide (FAD), respectively, with Asp396 neighboring Arg554. Herein, we probed the roles of these three residues in modification of FAD to 8-formyl-FAD. Replacement of Arg87 or Arg554 with Lys or Ala decreased and abolished the modification, respectively. Replacement of Asp396 with Ala or Asn lowered the modification rate. The observation of unusual effects of maintaining pH 7.0 on the modification in R87K, R554K, and D396 variants indicates initial and subsequent processes with different pH dependencies. Comparison of the initial process at pH 4.5 and 7.0 suggests that the microenvironment around Arg87 and the protonation state of Asp396 affect the initial process in the native enzyme. Comparison of the crystal structures of native and R554 variants showed that the replacements had minimal effect on catalytic site structure. The positively charged Arg87 might contribute to the formation of an anionic quinone-methide tautomer intermediate, while the positively charged Arg554, in collaboration with the negatively charged Asp396, might stabilize this intermediate and form a hydrogen bonding network with the N(5)/O(4) region, thereby facilitating efficient FAD modification.

Books etc

  • Epigenetics
    MASAYA OKI
    Epigenetics in Saccharomyces cerevisiae
     Sep.  2008

Conference Activities & Talks

  • 高次クロマチン構造境界領域形成機構の解析
    沖 昌也
     Jan.  2008