Cell
Volume 61, Issue 3, 4 May 1990, Pages 505-514
Journal home page for Cell

Article
Modular structure of a chicken lysozyme silencer: Involvement of an unusual thyroid hormone receptor binding site

https://doi.org/10.1016/0092-8674(90)90532-JGet rights and content

Abstract

Silencer elements, by analogy to enhancer elements, function independently of their position and orientation. We show that the chicken lysozyme silencer S-2.4 kb has many other characteristics in common with enhancer elements. The silencer is comprised of modules that independently repress gene activity-repression being increased synergistically when different or identical modules are combined. Repression is effective both on a complete and on a minimal promoter consisting of a TATA box only. One silencer module is bound in vitro by a 75–93 kd protein, termed NeP1; the other can be bound either by the product of the oncogene v-erbA or by the thyroid hormone receptor. This erbA binding site is unusual in that the palindromic sequence is inverted.

References (62)

  • C.M. Gorman et al.

    Negative regulation of viral enhancers in undifferentiated embryonic stem cells

    Cell

    (1985)
  • S. Green et al.

    Nuclear receptors enhance our understanding of transcription regulation

    Trends Genet.

    (1988)
  • D.A. Hager et al.

    Elution of proteins from sodium dodecylsulfate-polyacrylamide gels, removal of sodium dodecylsulfate and renaturation of enzymatic activity: results with sigma subunit of E. coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymes

    Anal. Biochem.

    (1980)
  • A. Hata et al.

    Tandemly reiterated negative enhancer-like elements regulate transcription of a human gene for the large subunit of calcium-dependent protease

    J. Biol. Chem.

    (1989)
  • J.F.-X. Hofmann et al.

    RAP-1 factor is necessary for DNA loop formation in vitro at the silent mating type locus HML

    Cell

    (1989)
  • V. Kumar et al.

    The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer

    Cell

    (1988)
  • S.L. McKnight

    Functional relationships between transcriptional control signals of the thymidine kinase gene of herpes simplex virus

    Cell

    (1982)
  • F.J. Rauscher et al.

    A common DNA binding site for Fos protein complexes and transcription factor AP-1

    Cell

    (1988)
  • C.A. Rosen et al.

    Location of cis-acting regulatory sequences in the human T cell lymphotropic virus type III (HTLV-III/LAV) long terminal repeat

    Cell

    (1985)
  • M. Takimoto et al.

    fos/jun and octamer-binding protein interact with a common site in a negative element of the human c-myc gene

    J. Biol. Chem.

    (1989)
  • S.Y. Tsai et al.

    Cooperative binding of steroid hormone receptors contributes to transcriptional synergism at target enhancer elements

    Cell

    (1989)
  • J. Altschmied et al.

    Cooperative interaction of chicken lysozyme enhancer sub-domains partially overlapping with a steroid receptor binding site

    Nucl. Acids Res.

    (1989)
  • A. Baniahmad et al.

    Activity of two different silencer elements of the chicken lysozyme gene can be compensated by enhancer elements

    EMBO J.

    (1987)
  • H. Beug et al.

    Erythroblast cell lines transformed by a temperature-sensitive mutant of avian erythroblast virus: a model system to study erythroid differentiation in vitro

    J. Cell. Physiol. Suppl.

    (1982)
  • A.R. Buchman et al.

    Connections between transcriptional activators, silencers, and telomeres as revealed by functional analysis of a yeast DNA-binding protein

    Mol. Cell. Biol.

    (1988)
  • K. Damm et al.

    Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist

    Nature

    (1989)
  • R.M. Evans

    The steroid and thyroid hormone receptor superfamily

    Science

    (1988)
  • M. Fried et al.

    Equilibria and kinetics of Lac repressor operator interactions by polyacrylamide gel electrophoresis

    Nucl. Acids Res.

    (1981)
  • H.P. Fritton et al.

    Alternative sets of DNasel-hypersensitive sites characterize the various functional states of the chicken lysozyme gene

    Nature

    (1984)
  • T. Fujita et al.

    Evidence for a nuclear factor(s), IRF-1, mediating induction and silencing properties to human IFN-β gene

    EMBO J.

    (1988)
  • M.M. Garner et al.

    A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: application to components of the E. coli lactose operon regulatory system

    Nucl. Acids Res.

    (1981)
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