In vitro assembly of a ribonucleoprotein particle corresponding to the platform domain of the 30S ribosomal subunit
| Autor: | Sultan Ch. Agalarov, V.D. Vasiliev, Alexander S. Spirin, E. N. Zheleznyakova, L. A. Zheleznaya, O. M. Selivanova, N. I. Matvienko |
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| Rok vydání: | 1998 |
| Předmět: |
Ribosomal Proteins
Protein Folding Multidisciplinary Base Sequence Transcription Genetic Eukaryotic Large Ribosomal Subunit Thermus thermophilus Molecular Sequence Data Ribonucleoprotein particle Biology Biological Sciences Molecular biology Ribosome 5S ribosomal RNA Microscopy Electron RNA Bacterial Ribosomal protein RNA Ribosomal RNA Ribosomal 16S Biophysics Escherichia coli Nucleic Acid Conformation 30S Eukaryotic Small Ribosomal Subunit 50S |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 95(3) |
| ISSN: | 0027-8424 |
| Popis: | A fragment of the 16S RNA of Thermus thermophilus corresponding to the central domain (nucleotides 547–895) has been prepared by transcription in vitro . Incubation of this fragment with the total 30S ribosomal proteins has resulted in the formation of a compact 12S ribonucleoprotein particle. This particle contained five T. thermophilus proteins corresponding to Escherichia coli ribosomal proteins S6, S8, S11, S15, and possibly S18, all of which were previously shown to interact with the central domain of the 16S RNA and to be localized in the platform (side bulge) of the 30S ribosomal subunit. When examined by electron microscopy, isolated particles have an appearance that is similar in size and shape to the corresponding morphological features of the 30S subunit. We conclude that the central domain of the 16S RNA can independently and specifically assemble with a defined subset of ribosomal proteins into a compact ribonucleoprotein particle corresponding to the platform (side bulge) of the 30S subunit. |
| Databáze: | OpenAIRE |
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