Surface topography of the 30 s Escherichia coli ribosomal subunit: reactivity towards fluorescein isothiocyanate
| Autor: | Charles R. Cantor, Kuei-Huang Huang |
|---|---|
| Rok vydání: | 1972 |
| Předmět: |
Electrophoresis
Conformational change Protein Conformation Protein subunit Phenylalanine Ribosome chemistry.chemical_compound Structure-Activity Relationship Bacterial Proteins Structural Biology Escherichia coli Reactivity (chemistry) Fluorescein isothiocyanate Molecular Biology Polyacrylamide gel electrophoresis Carbon Isotopes Ribosomal RNA Hydrogen-Ion Concentration Fluoresceins Biochemistry chemistry Isothiocyanate Biophysics Adsorption Ribosomes Thiocyanates |
| Zdroj: | Journal of molecular biology. 67(2) |
| ISSN: | 0022-2836 |
| Popis: | Celite-adsorbed fluoreseein isothiocyanate has been reacted with 30 s and 70 s ribosomes. At pH 9.0, approximately 12 dyes are found attached to the 30 s ribosomes and 11 to the 70 s ribosomes. When the subunits of the latter are separated, only 3 dyes are found attached to the 30 s particle. In all cases, virtually full biological activity is maintained. The detailed pattern of protein reactivity has been assessed by two-dimensional acrylamide gel electrophoresis. Most of the proteins of the isolated 30 s particle are reactive towards fluoreseein isothiocyanate. In contrast, many of these are protected when the reactivity of the 30 s moiety of the 70 s particle is examined. From the detailed results, a number of tentative conclusions about ribosome topography can be drawn. For example, proteins P1, P3, P4a and P15 appear to be definitely exposed in both 30 s and 70 s particles. P4b is almost certainly buried in both. P4, P8, P10, P10a, P11 and P13 are strongly shielded by the 50 s particle. One 30 s protein, P15, is much more strongly labeled in the 70 s particle than in the free 30 s. This indicates that the 30 s particle undergoes a conformational change when it combines with the 50 s particle. |
| Databáze: | OpenAIRE |
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