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Article Dans Une Revue Molecular and Cellular Biology Année : 1992

Zinc Fingers and Other Domains Cooperate in Binding of Drosophila sry 1 and 8 Proteins at Specific Chromosomal Sites

Résumé

The closely related Drosophila serendipity (siy) 13 and 8 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 8 protein fused to 1-galactosidase and expressed in Drosophila transgenic lines. Results show that the 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.
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hal-03064569 , version 1 (28-10-2022)

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Stéphane Noselli, Francois Payre, Alain Vincent. Zinc Fingers and Other Domains Cooperate in Binding of Drosophila sry 1 and 8 Proteins at Specific Chromosomal Sites. Molecular and Cellular Biology, 1992, 12 (2), pp.724-733. ⟨10.1128/mcb.12.2.724-733.1992⟩. ⟨hal-03064569⟩
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