Isolation and Initial Characterization of GBF,a Novel DNA-Binding Zinc Finger Protein That Binds to the GC-Rich Binding Sites of the HIV-1 Promoter

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Author(s)

    • Suzuki Toru SUZUKI Toru
    • Department of Developmental Biology,Department of Cellular Biology,Institute of Molecular and Cellular Biosciences,The University of Tokyo.
    • Yamamoto Tohru YAMAMOTO Tohru
    • Department of Developmental Biology,Department of Cellular Biology,Institute of Molecular and Cellular Biosciences,The University of Tokyo.
    • NAGAI Ryouzo
    • Second Department of Internal Medicine,Gunma University School of Medicine.
    • YAZAKI Yoshio
    • Third Department of Internal Medicine,Faculty of Medicine,The University of Tokyo.
    • HORIKOSHI Masami
    • Department of Developmental Biology,Department of Cellular Biology,Institute of Molecular and Cellular Biosciences,The University of Tokyo.

Abstract

Human immunodeficiency virus (HIV) and its clinical syndrome, acquired immune deficiency syndrome (AIDS), are one of the world's most prominent health problems. To understand the mechanisms underlying HIV transcription and thereby its propagation, we have focused on the molecular interactions at the GC-rich binding sites of the HIV-1 core promoter, a region important for HIV-1 transcription. Previous biochemical studies have shown that Spl, a zinc finger transcription factor initially isolated as a cellular factor binding that binds to the SV40 early promoter GC-rich sequence, binds to the HIV-1 GC-rich binding sites due to sequence similarities. However, the HIV-1 GC-rich binding sites are considerably different from the Spl consensus binding sequence, and recent genetic studies have shown the lack of regulation by Spl in numerous genes thought to be regulated by that factor in the past. We reasoned that other factors may bind to the HIV-1 GC-rich binding sites. Using the native HIV-1 GC-rich binding sequence as the bait, genetic screening for interacting factors was performed by the yeast one-hybrid method. A cDNA encoding a novel zinc finger protein named GBF, G<sub>-</sub>C-rich sites b<sub>-</sub>inding f<sub>-</sub>actor, was isolated from a human peripheral blood leukocyte library. Primary structure analysis of GBF revealed a C<sub>2</sub>H<sub>2</sub> Krüppel-type zinc finger at its C-terminus, and putative acidic and proline-rich domains at its N-terminus. We also show that GBF belongs to a subgroup of Krüppel-type zinc fingers distinct from Spl. By directly addressing interactions at the HIV-1 GC-rich binding sites, our present study sheds new light on molecular interactions at the HIV-1 promoter.

Journal

  • The Journal of Biochemistry

    The Journal of Biochemistry 124(2), 389-395, 1998-08-01

    The Japanese Biochemical Society

References:  28

Codes

  • NII Article ID (NAID)
    10005848564
  • NII NACSIS-CAT ID (NCID)
    AA00694073
  • Text Lang
    ENG
  • Article Type
    ART
  • ISSN
    0021924X
  • NDL Article ID
    4540156
  • NDL Source Classification
    ZR2(科学技術--生物学--生化学)
  • NDL Call No.
    Z53-B472
  • Data Source
    CJP  NDL  J-STAGE 
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