Identification of a 16-S RNA Fragment Crosslinked to Protein S1 within Escherichia coli Ribosomal 30-S Subunits by the Use of a Crosslinking Reagent: Ethyl 4-Azidobenzoylaminoacetimidate
| Autor: | Bernard Ehresmann, Régine Millon, Jean-Pierre Ebel, Claude Backendorf, Martin Olomucki, Barbara Golinska |
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| Rok vydání: | 2005 |
| Předmět: |
Ribosomal Proteins
Macromolecular Substances macromolecular substances Plasma protein binding Biology medicine.disease_cause Biochemistry Ribosomal protein Imidoesters Escherichia coli medicine Ribonuclease T1 Oligoribonucleotides Base Sequence technology industry and agriculture RNA Ribosomal RNA Cross-Linking Reagents RNA Ribosomal Reagent Ribosomes Protein Binding |
| Zdroj: | European Journal of Biochemistry. 115:479-484 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1981.tb06227.x |
| Popis: | The bifunctional reagent ethyl 4-azidobenzoylaminoacetimidate was used to crosslink specifically ribosomal protein S1 to 16-S RNA within 30-S subunits. The reagent was attached to isolated protein S1. The modified protein was reassociated with protein-S1-depleted 30-S subunits and then crosslinked to the RNA molecule. The covalently bound 16-S RNA-protein S1 complex was isolated and the RNA fragment C-U-A-A-C-G-C-G-U-U-A-A-G-U-C-G-A-C-C-G-C-C-U-G-G-G-G-A-G (positions 861-889) was characterized to be crosslinked to protein S1. |
| Databáze: | OpenAIRE |
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