High-resolution proton magnetic resonance study of the secondary structure of the 3'-terminal 49-nucleotide fragment of 16S rRNA from Escherichia coli
| Autor: | R A Baan, P.H. Van Knippenberg, E. Van Leerdam, C.W. Hilbers, R. Van Charldorp, Leendert Bosch |
|---|---|
| Rok vydání: | 1977 |
| Předmět: |
chemistry.chemical_classification
Messenger RNA Magnetic Resonance Spectroscopy Multidisciplinary Hydrogen Bonding Ribosomal RNA medicine.disease_cause 16S ribosomal RNA Ribosome Crystallography chemistry RNA Ribosomal Ribosomal protein Escherichia coli medicine Nucleic Acid Conformation Nucleotide Protein secondary structure Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 74:1028-1031 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.74.3.1028 |
| Popis: | The 3' terminus of 16S rRNA has been implicated in the recognition of mRNA's by the ribosome. A fragment containing the 3'-terminal 49 nucleotides cleaved from the rRNA by cloacin DF13 was isolated in a pure form. The secondary structure of this fragment has been studied by measuring the high-resolution proton magnetic resonance spectra. The resonances observed at low field can be assigned to hydrogen-bonded iminoprotons of base-pairs present in the fragment. From the data we conclude that the rRNA fragment, under the conditions used, exists as a hairpin consisting of eight intramolecular base-pairs, the 3'-terminal dodecanucleotide being unpaired. The implications of these findings with respect to the function of the ribosomal protein S1 are discussed. |
| Databáze: | OpenAIRE |
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