Effects on N-Glycosylation and Inositol on the ER Stress Response in Yeast Saccharomyces cerevisiae

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Abstract

<I>IRE1</I> and <I>HAC1</I> are essential for the unfolded protein response in the endoplasmic reticulum (ER). <I>IRE1</I>- and <I>HAC1</I>-disruptants require high concentrations of inositol for its normal growth. The <I>ALG6</I>, <I>ALG8</I>, and <I>ALG10</I> genes encode the glucosyltransferases necessary for the completion of the synthesis of the lipid-linked oligosaccharide used for the asparagine-linked glycosylation of proteins in that order. Here we show that, given a combination of the <I>hac1</I> defect with a disruption of <I>ALG6</I>, <I>ALG8</I>, and <I>ALG10</I>, no strains grow on inositol-free medium. However, the growth defect of the <I>hac1</I>-<I>alg10</I> double disrupted was partially, but significantly, suppressed by the addition of inositol to the medium. These results indicate that inositol, according to the numbers of glucose residues in the oligosaccharide, plays an important role in the stress response and quality control of glycoproteins in the ER.

Journal

  • Bioscience, Biotechnology, and Biochemistry

    Bioscience, Biotechnology, and Biochemistry 69(7), 1274-1280, 2005-07-23

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

References:  30

Cited by:  1

Codes

  • NII Article ID (NAID)
    130000030267
  • NII NACSIS-CAT ID (NCID)
    AA10824164
  • Text Lang
    ENG
  • Article Type
    Journal Article
  • ISSN
    09168451
  • NDL Article ID
    7378333
  • NDL Source Classification
    ZR7(科学技術--農林水産--農産) // ZR2(科学技術--生物学--生化学) // ZP1(科学技術--化学・化学工業)
  • NDL Call No.
    Z53-G223
  • Data Source
    CJP  CJPref  NDL  J-STAGE 
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