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Molecular interactions between ribosomal proteins--a study of S4-S9 interaction.
Prakash, V. (1991) Molecular interactions between ribosomal proteins--a study of S4-S9 interaction. Indian Journal of Biochemistry & Biophysics, 28 (5-6). pp. 374-80. ISSN 0301-1208
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Abstract
The ribosomal proteins S4 and S9 were isolated from the 30S ribosomal subunit of Escherichia coli to greater than 95% purity and characterized in the reconstitution buffer. Neither of the proteins indicated any tendency to self associate at 3 degrees C in the concentration range studied. At higher temperatures (greater than 20 degrees C), protein S9 forms a significant amount of a soluble aggregate as seen from the sedimentation velocity and sedimentation equilibrium experiments. From an analysis of the solution mixture of S4 and S9 at 1:1.08 molar concentration ratio by sedimentation velocity experiment, an s20,w value of 1.77 +/- 0.02S was obtained. A fast moving component which accounts for approximately 20% of the mass was also observed. Increasing the concentration of S9 does not alter the observed s20w value significantly for that component which could be followed. A detailed analysis of the data obtained at 3 degrees C from sedimentation equilibrium experiments on mixtures of the proteins indicated that a species of molecular weight greater than either of the two proteins was present. The proteins were found to interact with a mean equilibrium constant of association of 3.66 +/- 2.39 x 10(4) M-1 and a Gibbs free energy of interaction, delta Go = -5.8 kcal/mole at 3 degrees C in TMKD buffer. This information helps in understanding the energetics of the 30S ribosomal subunits of E. coli.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ribosomal proteins, molecular interactions |
| Subjects: | 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins |
| Divisions: | Protein Chemistry and Technology |
| Depositing User: | Food Sci. & Technol. Information Services |
| Date Deposited: | 15 Nov 2021 05:04 |
| Last Modified: | 01 Jun 2022 11:04 |
| URI: | http://ir.cftri.res.in/id/eprint/2324 |
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