Proceedings of the National Academy of Sciences · 1993 · 38 citations · 23 references
Life SciencesGeneticsMolecular BiologyChromatin StructureGene ExpressionNucleic Acid BiochemistryChromatinNucleic Acid-protein InteractionsProtein-nucleic Acid InteractionsRna LocalizationRna-binding ProteinsRna-protein InteractionsBinding StudiesSingle-strand Dna Binding ProteinsSingle-stranded Dna Binding ProteinsSingle-stranded Dna RecognitionSingle-stranded Dna-binding ProteinsSingle-stranded Nucleic Acid Binding ProteinsStructure-specific Recognition
We have isolated a Drosophila melanogaster cDNA encoding a high-mobility-group (HMG) box-containing protein. This protein shares 50% amino acid identity with the human putative structure-specific recognition protein, hSSRP. The gene encoding the D. melanogaster homolog, DssRP, is developmentally regulated and is expressed most abundantly in ovaries (nurse cells in particular). The protein is localized in nuclei and is particularly abundant in the nucleolus. In vitro binding studies using DssRP produced in bacteria showed that, despite expectation, the protein does not bind to structured DNA. Instead, it binds to single-stranded DNA and RNA, with highest affinity to nucleotides G and U.
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Basic local alignment search tool
Stephen F. Altschul, Warren Gish, Webb Miller et al. · Journal of Molecular Biology · 1990 · 94.5K citations
Diethard Tautz, Christine Pfeifle · Chromosoma · 1989 · 2.6K citations