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Genomic Cloning and Promoter Analysis of the Mouse 105-kDa Heat Shock Protein (HSP105) Gene

https://doi.org/10.1006/bbrc.1999.0283Get rights and content

Abstract

The 105-kDa heat shock protein (HSP105) is a member of the high-molecular-mass heat shock protein family. We have isolated and characterized the mouse HSP105 gene including about 1.2 kb of the 5′-flanking region. The mouse HSP105 gene spans about 22 kb, consisting of 18 exons separated by 17 introns. Southern blotting analysis revealed the existence of a single copy of HSP105. Primer extension analysis revealed that the transcription initiation site was located 165 bp upstream of the ATG translation initiation codon. The 5′-promoter region of the HSP105 gene contained a TATA box, a CAAT box, an inverted CAAT box, and two GC boxes. Two heat shock element (HSE) sequences were found as four nGAAn repeats at nt −64 and nt −128. Promoter analysis using deletion derivatives revealed that a minimal region which contained the two consensus HSE sequences was active in response to heat shock and also for constitutive expression of the gene.

References (31)

  • E.A. Craig et al.

    Cell

    (1994)
  • T. Hatayama et al.

    Biochem. Biophys. Res. Commun.

    (1994)
  • T. Hatayama et al.

    Biochem. Biophys. Res. Commun.

    (1994)
  • T. Hatayama et al.

    Biochem. Biophys. Res. Commun.

    (1986)
  • K. Honda et al.

    Biochem. Biophys. Res. Commun.

    (1989)
  • K. Yasuda et al.

    J. Biol. Chem.

    (1995)
  • D. Lee-Yoon et al.

    J. Biol. Chem.

    (1995)
  • S. Storozhenko et al.

    FEBS Lett.

    (1996)
  • Y. Kaneko et al.

    J. Biol. Chem.

    (1997)
  • Y. Kaneko et al.

    Gene

    (1997)
  • M.L. Just et al.

    Dev. Biol.

    (1997)
  • K.S. Chung et al.

    Gene

    (1998)
  • N. Plesofsky-Vig et al.

    J. Biol. Chem.

    (1998)
  • F.L. Graham et al.

    Virology

    (1973)
  • P. Senapathy et al.

    Methods Enzymol.

    (1990)
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    To whom correspondence should be addressed at Department of Biochemistry, Kyoto Pharmaceutical University, 5 Nakauchi-cho, Misasagi, Yamashina-ku, Kyoto 607-8414, Japan. Fax: 075-595-4758. E-mail:[email protected].

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