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Molecular interactions between ribosomal proteins -- an analysis of S7-S9, S7-S19, S9-S19 and S7-S9-S19 interactions.

IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore

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Title Molecular interactions between ribosomal proteins -- an analysis of S7-S9, S7-S19, S9-S19 and S7-S9-S19 interactions.
 
Creator Prakash, V.
 
Subject 13 Molecular Biochemistry
03 Proteins
 
Description Ribosomal proteins S7, S9 and S 19 from Escherichia coli have been studied by the sedimentation equilibrium technique for possible intermolecular interaction between pairs of proteins as well as in a mixture of 3 proteins. The proteins were isolated to a purity greater than 95% and were characterized in the reconstitution buffer. It was observed that none of the proteins has a tendency to self-associate in the concentration range studied in the temperature range 3–6°C. Protein S9 behaves differently in the presence of other proteins. Analysis of the sedimentation equilibrium data for S7–S9, S9– S19 and S7–S9–S19 complexes revealed the need for considering the presence of a component of higher molecular weight in the system along with the monomers and their complexes to provide a meaningful curve-fitting of the data. Proteins S7 and S19 were found to interact with an equilibrium constant of association of 3 ± 2 × 104 M–1 at 3°C with a Gibbs free energy of interaction ΔG° of -5·7 kcal/mol. These data are useful for the consideration of the stabilization of the 30S subunit through protein-protein interactions and also help in building a topographical model of the proteins of the small subunit from an energetics point of view.
 
Date 1988
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/4666/1/J.%20Biosci.%2C%20Vol.%2013%2C%20Number%203%2C%20September%201988%2C%20pp.%20329%E2%80%93342.pdf
Prakash, V. (1988) Molecular interactions between ribosomal proteins -- an analysis of S7-S9, S7-S19, S9-S19 and S7-S9-S19 interactions. Journal of Biosciences, 13 (3). pp. 329-342.