ArticleNucleic acids research1998
Activities of the Sex-lethal protein in RNA binding and protein:protein interactions.
Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
- RNA-Binding Proteins (RBPs) and Circular RNA Biogenesis.Advances in experimental medicine and biology · 2025Review
- MicroSalmon: A Comprehensive, Searchable Resource of Predicted MicroRNA Targets and 3'UTR Cis-Regulatory Elements in the Full-Length Sequenced Atlantic Salmon Transcriptome.Non-coding RNA · 2021Article
- Precise staging of beetle horn formation in Trypoxylus dichotomus reveals the pleiotropic roles of doublesex depending on the spatiotemporal developmental contexts.PLoS genetics · 2019Article
- Drosophila Sister-of-Sex-lethal reinforces a male-specific gene expression pattern by controlling Sex-lethal alternative splicing.Nucleic acids research · 2019Article
- Article
- Promiscuity in post-transcriptional control of gene expression: Drosophila sex-lethal and its regulatory partnerships.FEBS letters · 2017Review
- Biochemical and functional analysis of Drosophila-sciara chimeric sex-lethal proteins.PloS one · 2013Article
- Functioning of the Drosophila Wilms'-tumor-1-associated protein homolog, Fl(2)d, in Sex-lethal-dependent alternative splicing.Genetics · 2008Article
- Formation of a Tap/NXF1 homotypic complex is mediated through the amino-terminal domain of Tap and enhances interaction with nucleoporins.Molecular biology of the cell · 2008Article
- The master switch gene sex-lethal promotes female development by negatively regulating the N-signaling pathway.Developmental cell · 2007Article
- The role of RNA structure in the interaction of U1A protein with U1 hairpin II RNA.RNA (New York, N.Y.) · 2006Article
- The gene Sex-lethal of the Sciaridae family (order Diptera, suborder Nematocera) and its phylogeny in dipteran insects.Genetics · 2004Article
- Article
- A co-repressor assembly nucleated by Sex-lethal in the 3'UTR mediates translational control of Drosophila msl-2 mRNA.The EMBO journal · 2003Article
- RNA binding protein sex-lethal (Sxl) and control of Drosophila sex determination and dosage compensation.Microbiology and molecular biology reviews : MMBR · 2003Review
- The KH domains of Xenopus Vg1RBP mediate RNA binding and self-association.RNA (New York, N.Y.) · 2002Article
- Characterization of interactions among the Cef1p-Prp19p-associated splicing complex.RNA (New York, N.Y.) · 2002Article
- Article
- HuD RNA recognition motifs play distinct roles in the formation of a stable complex with AU-rich RNA.Molecular and cellular biology · 2000Article
- An N-terminal truncation uncouples the sex-transforming and dosage compensation functions of sex-lethal.Molecular and cellular biology · 1999Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Drosophila sex determination gene Sex-lethal (Sxl) controls its own expression, and the expression of downstream target genes such as transformer , by regulating pre-mRNA splicing and mRNA translation. Sxl codes an RNA-binding protein that consists of an N-terminus of approximately 100 amino acids, two 90 amino acid RRM domains, R1 and R2, and an 80 amino acid C-terminus. In the studies reported here we have examined the functional properties of the different Sxl protein domains in RNA binding and in protein:protein interactions. The two RRM domains are responsible for RNA binding. Specificity in the recognition of target RNAs requires both RRM domains, and proteins which consist of the single domains or duplicated domains have anomalous RNA recognition properties. Moreover, the length of the linker between domains can affect RNA recognition properties. Our results indicate that the two RRM domains mediate Sxl:Sxl protein interactions, and that these interactions probably occur both in cis and trans. We speculate that cis interactions between R1 and R2 play a role in RNA recognition by the Sxl protein, while trans interactions stabilize complex formation on target RNAs that contain two or more closely spaced binding sites. Finally, we show that the interaction of Sxl with the snRNP protein Snf is mediated by the R1 RRM domain.
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