ArticleProceedings of the National Academy of Sciences of the United States of America1996
Purification and physical properties of the male and female double sex proteins of Drosophila.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- DMRT Transcription Factors in the Control of Nervous System Sexual Differentiation.Frontiers in neuroanatomy · 2022Review
- Doublesex Evolution Is Correlated with Social Complexity in Ants.Genome biology and evolution · 2018Article
- Double nexus--Doublesex is the connecting element in sex determination.Briefings in functional genomics · 2015Review
- Molecular cloning of Pcc-dmrt1s and their specific expression patterns in Pengze crucian carp (Carassius auratus var. Pengze) affected by 17α-methyltestosterone.Fish physiology and biochemistry · 2014Article
- Systems behavior: of male courtship, the nervous system and beyond in Drosophila.Current genomics · 2008Article
- Genomic and functional studies of Drosophila sex hierarchy regulated gene expression in adult head and nervous system tissues.PLoS genetics · 2007Article
- Vertebrate DM domain proteins bind similar DNA sequences and can heterodimerize on DNA.BMC molecular biology · 2007Article
- Sex-, stage- and tissue-specific regulation by a mosquito hexamerin promoter.Insect molecular biology · 2006Article
- Regulation of sexual dimorphism: mutational and chemogenetic analysis of the doublesex DM domain.Molecular and cellular biology · 2006Article
- Functional and genetic characterization of the oligomerization and DNA binding properties of the Drosophila doublesex proteins.Genetics · 1996Article
- Sex-specific and non-sex-specific oligomerization domains in both of the doublesex transcription factors from Drosophila melanogaster.Molecular and cellular biology · 1996Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The double sex gene (dsx) encodes two proteins, DSX(M) and DSX(F), that regulate sex-specific transcription in Drosophila. These proteins bind target sites in DNA from which the male-specific DSX(M) represses and the female-specific DSX(F) activates transcription of yolk protein (Yp) genes. We investigated the physical properties of these DSX proteins, which are identical in their amino-terminal 397 residues but are entirely different in their carboxyl-terminal sequences (DSX(F), 30 amino acids; DSX(M), 152 amino acids). DSX(M) and DSX(F) were overexpressed in cultured insect cells and purified to near homogeneity. Gel filtration chromatography and glycerol gradient sedimentation showed that at low concentrations both proteins are dimers of highly asymmetrical shape. The axial ratios are approximately 18:1 (DSX(M), 860 X 48 angstroms; DSX(F), 735 X 43 angstroms). At higher concentrations, the proteins form tetramers. Through use of a novel, double crosslinking assay (protein-DNA plus protein-protein), we demonstrated that a DNA regulatory site binds to both monomers of the DSX dimer and to only two monomers of the tetramer. Furthermore, binding another DNA molecule to what we presume is the second and identical site in the tetramer dramatically shifts the equilibrium from tetramers to dimers. These oligomerization and DNA binding properties are indistinguishable between the male and female proteins.
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