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Study on the development and differentiation of endoplasmic reticulum of yeast from the view point of lipid synthesis.

Research Project

Project/Area Number 07456045
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field 応用微生物学・応用生物化学
Research InstitutionThe University of Tokyo

Principal Investigator

OHTA Akinori  The University of Tokyo, Graduate School Agriculture & Agricultural Sciences, Department of Biotechnology, Associate Professor, 大学院・農学生命科学研究科, 助教授 (30125885)

Project Period (FY) 1995 – 1996
Project Status Completed (Fiscal Year 1996)
Budget Amount *help
¥7,800,000 (Direct Cost: ¥7,800,000)
Fiscal Year 1996: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 1995: ¥6,400,000 (Direct Cost: ¥6,400,000)
KeywordsSaccharomyces cerevisiae / phospholipid synthesis / endoplasmic reticulum / yeast / phosphatidylserine synthase / Saccharomyces cerevisiae / りん脂質合成 / リン脂質 / ホスファチジルセリン / ホスファチジレエタノールアミン / ホスファチジルコリン / CDP-エタノールアミン
Research Abstract

The aim of this research is to elucidate the mechanism of development and differentiation of endoplasmic reticulum (ER) of Saccharomyces cerevisiae, especially in relation to the organization of phospholipid synthetic enzymes that reside mainly in ER.Results are as follows,
(1) We succeeded in development of a gentle subcellular fractionation method that employs D-sorbitol density gradient centrifugation.
(2) We prepared antibodies specific to N-terminaus of phosphatidylserine synthase (PSS) and specific to phosphorylethanolamine cytidylyltransferase of S.cervisiae.
(3) A series of fusion genes coding for N-terminal regions of PSS and Escherichia coli beta-galactosidase were constructed. In addition to them, a deletion PSS that lacks N-terminal 50 amino acid residues was constructed. From their localization analysis, both the hydrophilic N-terminal region and a hydrophobic region from 115th to 129th were necessary for the proper ER localization of PSS.
(4) A pss ect mutant contained low amaount of phosphatidylethanolamine (PE). This double mutant was temperature-sensitive in growth and had altered ER structures, suggesting the necessity of PE in proper ER morphology.

Report

(3 results)
  • 1996 Annual Research Report   Final Research Report Summary
  • 1995 Annual Research Report
  • Research Products

    (4 results)

All Other

All Publications (4 results)

  • [Publications] Rho Min-Seok: "Isolation and charactenzation of ECTI gene encoding CTP:phospharyl-ethanolamine cytidylyl trevsferase of Sacchavomyes cerevisiae" J.Biochem.120. 1040-1047 (1996)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Rho Min-Seok et al.: "Isolation and characterization of ECT1 gene encoding CTP : phosphorylethanolamine cytidylyltransferase of Saccharomyces cerevisiae." J.Biochem.120. 1040-1047 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1996 Final Research Report Summary
  • [Publications] Rho Min-Seok.: "Isolation and characterization of ECT1 gene encoding CTP:phosphorylethanolamine cytidylyl transferase of Saccharomyces cerevisiae." J.Biochem.120. 1040-1047 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] Pho Min-Suk: "Isolation and characterization of ECT1 gene encoding CTP:phosphoethanolamine cytidylyltransferase of Saccharomyces cerevisiae." Journal of Biological Chemistry. (発表予定). (1996)

    • Related Report
      1995 Annual Research Report

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Published: 1995-04-01   Modified: 2016-04-21  

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