Fub1p, a novel protein isolated by boundary screening, binds the proteasome complex

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Author(s)

    • Chen Bo CHEN Bo
    • Department of Applied Chemistry & Biotechnology, Graduate School of Engineering, University of Fukui
    • MANO Yasunobu
    • Department of Applied Chemistry & Biotechnology, Graduate School of Engineering, University of Fukui
    • JU Yunfeng
    • Department of Biochemistry, Faculty of Medical Science, University of Fukui
    • MIZUTANI Tetsuya
    • Department of Biochemistry, Faculty of Medical Science, University of Fukui
    • MIYAMOTO Kaoru
    • Department of Biochemistry, Faculty of Medical Science, University of Fukui
    • UCHIDA Hiroyuki
    • Department of Applied Chemistry & Biotechnology, Graduate School of Engineering, University of Fukui
    • OKI Masaya
    • Department of Applied Chemistry & Biotechnology, Graduate School of Engineering, University of Fukui

Abstract

Silenced chromatin domains are restricted to specific regions. Eukaryotic chromosomes are organized into discrete domains delimited by domain boundaries. From approximately 6,000 genes in <i>Saccharomyces cerevisiae</i>, we previously isolated 55 boundary genes. In this study, we focus on the molecular function of one of boundary genes, <i>YCR076C/FUB1</i> (<u>fu</u>nction of <u>b</u>oundary), whose function has not been clearly defined <i>in vivo</i>. Biochemical analysis of Fub1p revealed that it interacted with multiple subunits of the 20S proteasome core particle (20S CP). To further clarify the functional link between Fub1p and proteasome, several proteasome mutants were analyzed. Although only 20S CP subunits were isolated as Fub1p interactors, a genetic interaction was also observed for component of 19S regulatory particle (19S RP) suggesting involvement of Fub1p with the whole proteasome. We also analyzed the mechanism of boundary establishment by using proteasome composition factor-deficient strains. Deletion of <i>pre9</i> and <i>ump1</i>, whose products have effects on the 20S CP, resulted in a decrease in boundary function. Domain analyses of Fub1p identified a minimum functional domain in the C terminus that was essential for boundary establishment and showed a limited sequence homology to the human PSMF1, which is known to inhibit proteasome activity. Finally, boundary assay showed that human PSMF1 also exhibited boundary establishment activity in yeast. Our results defined the functional correlation between Fub1p and PSMF1.<br>

Journal

  • Genes & Genetic Systems

    Genes & Genetic Systems 86(5), 305-314, 2011-10-25

    The Genetics Society of Japan

References:  53

Codes

  • NII Article ID (NAID)
    10030209843
  • NII NACSIS-CAT ID (NCID)
    AA11077421
  • Text Lang
    ENG
  • Article Type
    ART
  • ISSN
    13417568
  • NDL Article ID
    023417414
  • NDL Call No.
    Z53-W539
  • Data Source
    CJP  NDL  IR  J-STAGE 
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