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Identification and functional analysis of cytoplasmic factors involved in nuclear protein transport

Research Project

Project/Area Number 05680612
Research Category

Grant-in-Aid for General Scientific Research (C)

Allocation TypeSingle-year Grants
Research Field Cell biology
Research InstitutionOsaka University

Principal Investigator

IMAMOTO Naoko  Osaka University Medical School, Department of Anatomy and Cell Biology, Assistant Professor, 医学部, 助手 (20202145)

Project Period (FY) 1993 – 1994
Project Status Completed (Fiscal Year 1994)
Budget Amount *help
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1994: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1993: ¥1,100,000 (Direct Cost: ¥1,100,000)
Keywordsnulclear transport / nuclear location signal / nuclear pore / in vitro transport system / in vitro輸送系 / 熱ショックタンパク質
Research Abstract

Targeting of karyophilic proteins to nuclear pores is known to require several cytoplasmic factors including the nuclear location signal (NLS) -binding protein. Using a digitonin-permeabilized cell-free transport assay, we have obtained a cytoplasmic fraction containing factors that specifically bind to karyophilic protein and support the nuclear binding step of the transport. Components in this fraction form a stable complex with the karyophile through interaction with NLS.Since this complex shows nuclear pore binding activity prior to nuclear entry in the absence of other cytosolic factors, we call it nuclear pore-targeting complex. It consists of karyophilic protein and four proteins of 54,56,66, and 90kDa. In our reconstitution experiments, a complex with 54 and 90kDa proteins is capable of targeting karyophiles to the nuclear pores.

Report

(3 results)
  • 1994 Annual Research Report   Final Research Report Summary
  • 1993 Annual Research Report
  • Research Products

    (10 results)

All Other

All Publications (10 results)

  • [Publications] Yumiko Okuno: "70-kDa heat shock cognate protein colocalizes with karyophilic proteins into the nucleus during their transport in vitro." Experimental Cell Research. 206. 134-142 (1993)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Taro Tachibana: "Loss of RCC1 leads to suppression of nuclear protein import in living cells" J.Biol.Chem.269. 24542-24545 (1994)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Nako lmamoto: "A karyophilic protein forms a stable complex with cutoplasmic components prior to nuclear pore binding." J.Biol.Chem.(in press).

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Yumiko Okuno: "70-kDa heat shock cognate protein colocalizes with karyophilic proteins into the nucleus during their transport in vitro." Experimental Cell Research. Vol.206. 134-142 (1993)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Taro Tachibana: "Loss of RCC1 leads to suppression of nuclear protein import in living cells." J.Biol.Chem.Vol.269. 24542-24545 (1994)

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Naoko Imamoto: "A karyophilic protein forms a stable complex with cytoplasmic components prior to nuclear pore binding." J.Biol.Chem.(in press).

    • Description
      「研究成果報告書概要(欧文)」より
    • Related Report
      1994 Final Research Report Summary
  • [Publications] Yumiko Okuno: "70-kDa heat shock cognate protein colocalizes with karyophilic proteins into the nucleus during their transport in vitro." Experimental Cell Research. 206. 134-142 (1993)

    • Related Report
      1994 Annual Research Report
  • [Publications] Taro Tachibana: "Loss of RCC1 leads to suppression of nuclear protein import in living cells" J.Biol.Chem.269. 24542-24545 (1994)

    • Related Report
      1994 Annual Research Report
  • [Publications] Naoko Imamoto: "A karyophilic protein forms a stable complex with cytoplasmic components prior to nuclear pore binding." J.Biol.Chem.(in press).

    • Related Report
      1994 Annual Research Report
  • [Publications] Okuno Yumiko: "70-kDa heat shock cognate protein colocalizes with karyophilic proteins into the nucleus during their transpart in vitro." Experimental Cell Research. 206. 134-142 (1993)

    • Related Report
      1993 Annual Research Report

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Published: 1993-04-01   Modified: 2016-04-21  

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