PMID: 7028091Aug 4, 1981Paper

Solution behavior of proteins L7/L12 from the 50S ribosomal subunit of Escherichia coli

Biochemistry
E G Kar, K C Aune

Abstract

The behavior of Escherichia coli 50S ribosomal subunit proteins L7/L12 has been investigated in ribosome reconstitution buffer, TMK buffer, by sedimentation equilibrium and analytical gel filtration. Contrary to previous reports that L7/L12 exists in solution solely as dimer species [Möller, W., Groene, A., Terhorst, C., & Amons, R. (1972) Eur J. Biochem. 25, 5], results presented here indicate that L7/L12 undergoes a monomer-dimer-tetramer self-association, with equal equilibrium constants of 3.5 x 10(4) M-1 obtained for the monomer-dimer and dimer-tetramer steps. These results yield standard Gibbs' free energies of -6.1 +/ 0.6 kcal/mol at 20 degrees C. The observed absence of temperature dependence of this interaction over the range 5-25 degrees C indicated a zero standard enthalpy of self-association. Gel filtration results are presented that confirm the highly elongated shape of the L7/L12 molecule. The data suggest the corresponding Stokes radii for the monomer, dimer, and tetramer are 21-23, 26-28, and 29-32 omicron A, respectively. The significance of these results is discussed.

References

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Citations

Jan 1, 1982·Progress in Biophysics and Molecular Biology·A Liljas
Jan 2, 1984·European Journal of Biochemistry·J A MaassenW Möller
May 1, 1973·Archives of Biochemistry and Biophysics·K C Aune
Mar 7, 2017·Biochemistry. Biokhimii︠a︡·I V MitroshinA G Gabdulkhakov

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