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  • The EMBO Journal (1998) 17, 2079 - 2085
  • doi:10.1093/emboj/17.7.2079

In vivo analysis of scaffold-associated regions in Drosophila: a synthetic high-affinity SAR binding protein suppresses position effect variegation

Franck Girard2, Bruno Bello1, Ulrich K. Laemmli3 and Walter J. Gehring1

  1. Department of Cell Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, France
  2. Present address: CNRS ERS155, 1919 route de Mende, 34033 Montpellier, France
  3. Department of Biochemistry and Molecular Biology, 30 Quai Ernest Ansermet Sciences II, 1211 Genève, Switzerland

Correspondence to:

Walter J. Gehring, E-mail: gehring@ubaclu.unibas.ch

Received 15 December 1997; Accepted 4 February 1998; Revised 29 January 1998

Scaffold-associated regions (SARs) were studied in Drosophila melanogaster by expressing a synthetic, high-affinity SAR-binding protein called MATH (multi-AT-hook), which consists of reiterated AT-hook peptide motifs; each motif is known to recognize a wide variety of short AT-rich sequences. MATH proteins were expressed specifically in the larval eye imaginal discs by means of the tetracycline-regulated transactivation system and tested for their effect on position effect variegation (PEV). MATH20, a highly potent SAR ligand consisting of 20 AT-hooks, was found to suppress whitemottled 4 variegation. This suppression required MATH20 expression at an early larval developmental stage. Our data suggest an involvement of the high AT-rich SARs in higher order chromatin structure and gene expression.

  • Keywords:

    • chromatin structure,
    • Drosophila,
    • PEV,
    • SAR