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Functional analysis of TAND (TAF N-terminal domain) that inhibits TBP : DNA interactions

Research Project

Project/Area Number 09680677
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field Molecular biology
Research InstitutionNara Institute of Science and Technology

Principal Investigator

KOKUBO Tetsuro  Nara Institute of Science and Technology, Graduate School of Biological Sciences, Associate Professor, バイオサイエンス研究科, 助教授 (10271587)

Co-Investigator(Kenkyū-buntansha) KASAHARA Kouji  Nara Institute of Science and Technology, Graduate School of Biological Sciences, バイオサイエンス研究科, 助手 (40304159)
三宅 剛司  奈良先端科学技術大学院大学, バイオサイエンス研究科, 助手 (00283937)
Project Period (FY) 1997 – 1998
Project Status Completed (Fiscal Year 1998)
Budget Amount *help
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 1998: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 1997: ¥2,100,000 (Direct Cost: ¥2,100,000)
Keywordstranscription / TFIID / general transcription factor / TAF / TAND / activation / transcriptional regulation
Research Abstract

TFIID is a multiprotein complex comprised of TBP and several TAFlls. Small N-terminal segments (TAND ; TAF N-terminal Domain) of Drosophila TAFll23O (dTAFll230) and yeast TAFll145 (yTAFll145) bind strongly to TBP and thereby inhibit TBP : DNA interactions. dTAFll230 TAND (dTAND) and yTAFll145 TAND (yTAND) were further divided into two subdomains, dTANDI (18-77 aa) & II(118-143 aa), and yTANDI (10-37 aa) & II(46-71 aa), respectively, that function cooperatively. More importantly, TANDI and TANDII compete with activators and TFIIA, respectively, for TBP binding. We also demonstrated the functional conservation between activation domains and TANDI.When fused to the DNA-binding domain, TANDI functions as an activation domain in yeast. Conversely, activation domains function as TANDI when TANDI is replaced with activation domains within TEIID.Furthermore, we show that the interaction with the concave surface of TBP is crucial for the functions of both activators and TAN DI.These results indicate that transcriptional activation steps include suppression of the inhibitory activity of TANDI by transcriptional activators.

Report

(3 results)
  • 1998 Annual Research Report   Final Research Report Summary
  • 1997 Annual Research Report
  • Research Products

    (11 results)

All Other

All Publications (11 results)

  • [Publications] Kotani T et al.: "Identification of highly conserved amino-terminal segments of dTAFII230 and yTAFII145 that are functionally interchangeable for inhibiting TBP : DNA interactions in vitro and in promoting yeast cell growth in vivo" Journal of Biological Chemistry. 273(48). 32254-32264 (1998)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Liu D et al: "Soluion Structure of a TBP-TAFII230 complex : Protein mimicry of the minor groove surface of the TATA box unwound by TBP" Cell. 94(5). 573-583 (1998)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Drysdale CM et al: "The Gen4p activation domain interacts specifically in vitro with RNA polymerase II holoenzyme, TFIID, and the Adap-Gen5p coactivator complex" Molecular and Cellular Biology. 18(3). 1711-1724 (1998)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Kokubo T et al: "The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein" Molecular and Cellular Biology. 18(2). 1003-1012 (1998)

    • Description
      「研究成果報告書概要(和文)」より
    • Related Report
      1998 Final Research Report Summary
  • [Publications] Kotani T et al: "Identification of highly conserved amino-terminal segments of dTAFII230 and yTAFII145 that are functionally interchangeable for inhibiting TBP:DNA interactions in vitro and in promoting yeast cell growth in vivo" Journal of Biological Chemistry. 273(48). 32254-32264 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] Liu D et al: "Solution structure of a TBP-TAFII230 complex: Protein mimicry of the minor groove surface of the TATA box unwound by TBP" Cell. 94(5). 573-583 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] Drysdale CM et al: "The Gcn4p activation domain interacts specifically in vitro with RNA polymerase II holoenzyme, TFIID, and the Adap-Gen5p coactivator complex" Molecular and Cellular Biology. 18(3). 1711-1724 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] Kokubo T et al: "The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein" Moleculas and Cellular Biology. 18(2). 1003-1012 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] Sakurai Y et al: "The cDNA cloning and molecular characterization of a snake venom platelet glycoprotein 1b-binding protein, Mamushigin, from Agkistrodon halys blomhoffii venom" Thromb.Haemost.79. 1199-1207 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] Drysdale CM et al: "The Gcn4p activation domain interacts specifically in vitro with RNA polymerase II holoenzyme,TFIID,and the Adap-Gcn5p coactivator complex." Mol.Cell.Biol.18(3). 1711-1724 (1998)

    • Related Report
      1997 Annual Research Report
  • [Publications] Kokubo T et al: "The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein" Mol.Cell.Biol.18(2). 1003-1012 (1998)

    • Related Report
      1997 Annual Research Report

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Published: 1997-04-01   Modified: 2016-04-21  

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