ArticleMolecular and cellular biology2006
Regulation of sexual dimorphism: mutational and chemogenetic analysis of the doublesex DM domain.
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 23 citations in OpenAlex.
- Article
- Batesian mimicry has evolved with deleterious effects of the pleiotropic gene doublesex.Scientific reports · 2020Article
- The ubiquity and ancestry of insect doublesex.Scientific reports · 2015Article
- Sex- and tissue-specific functions of Drosophila doublesex transcription factor target genes.Developmental cell · 2014Article
- The role of doublesex in the evolution of exaggerated horns in the Japanese rhinoceros beetle.EMBO reports · 2013Article
- A Wt1-Dmrt1 transgene restores DMRT1 to sertoli cells of Dmrt1(-/-) testes: a novel model of DMRT1-deficient germ cells.Biology of reproduction · 2013Article
- Doublesex target genes in the red flour beetle, Tribolium castaneum.Scientific reports · 2012Article
- Direct targets of the D. melanogaster DSXF protein and the evolution of sexual development.Development (Cambridge, England) · 2011Article
- Crystallographic analysis of a sex-specific enhancer element: sequence-dependent DNA structure, hydration, and dynamics.Journal of molecular biology · 2009Article
- Vertebrate DM domain proteins bind similar DNA sequences and can heterodimerize on DNA.BMC molecular biology · 2007Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Doublesex (dsx) is a transcription factor in Drosophila that regulates somatic sexual differentiation. Male- and female-specific splicing isoforms of DSX share a novel DNA-binding domain, designated the DM motif. Broadly conserved among metazoan sex-determining factors, the DM domain contains a nonclassical zinc module and binds in the DNA minor groove. Here, we characterize the DM motif by site-directed and random mutagenesis using a yeast one-hybrid (Y1H) system and extend this analysis by chemogenetic complementation in vitro. The Y1H system is based on a sex-specific Drosophila enhancer element and validated through studies of intersexual dsx mutations. We demonstrate that the eight motif-specific histidines and cysteines engaged in zinc coordination are each critical and cannot be interchanged; folding also requires conserved aliphatic side chains in the hydrophobic core. Mutations that impair DNA binding tend to occur at conserved positions, whereas neutral substitutions occur at nonconserved sites. Evidence for a specific salt bridge between a conserved lysine and the DNA backbone is obtained through the synthesis of nonstandard protein and DNA analogs. Together, these results provide molecular links between the structure of the DM domain and its function in the regulation of sexual dimorphism.
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