Open AccessZinc Fingers and Other Domains Cooperate in Binding of Drosophila sry β and δ Proteins at Specific Chromosomal Sites
Author(s) -
Stéphane Noselli,
François Payre,
Alaín Víncent
Publication year - 1992
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.12.2.724-733.1992
Subject(s) - polytene chromosome , zinc finger , biology , testis determining factor , drosophila (subgenus) , dna , genetics , dna binding protein , microbiology and biotechnology , gene , drosophila melanogaster , transcription factor , y chromosome
The closely related Drosophila serendipity (sry) beta and delta zinc finger proteins display consensus in vitro DNA recognition sequences differing by 4 of 13 nucleotide positions and bind in vivo to distinct sets of sites on polytene chromosomes. We compared the pattern of in vivo chromosomal binding of deleted forms of the sry delta protein fused to beta-galactosidase and expressed in Drosophila transgenic lines. Results show that the carboxy-terminal DNA-binding finger domain is required and sufficient for binding at specific chromosomal sites but that this binding does not nearly reproduce the wild-type pattern. An NH2-terminal domain of the sry delta protein is essential to its specificity of in vivo interaction with chromatin. In vitro and in vivo experiments using reciprocal finger swap between the sry beta and delta proteins suggest that the in vivo specificity is dependent on selective protein-protein contacts at defined chromosomal sites, in addition to DNA specific recognition.