A Drosophila single-strand DNA/RNA-binding factor contains a high-mobility-group box and is enriched in the nucleolus
| Autor: | Carole LaBonne, Dennis L. King, Tien Hsu, Fotis C. Kafatos |
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| Rok vydání: | 1993 |
| Předmět: |
Molecular Sequence Data
DNA Single-Stranded Biology chemistry.chemical_compound DDB1 Complementary DNA Gene expression Animals Drosophila Proteins Amino Acid Sequence RNA Messenger Nuclear protein Gene Gene Library Multidisciplinary Base Sequence Sequence Homology Amino Acid High Mobility Group Proteins RNA-Binding Proteins RNA Molecular biology Recombinant Proteins Cell Compartmentation Cell biology DNA-Binding Proteins Drosophila melanogaster chemistry Female Transcriptional Elongation Factors Cell Nucleolus DNA Drosophila Protein Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 90:6488-6492 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.90.14.6488 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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