Neutron scattering study of the 13 S fragment of 16 S RNA and its complex with ribosomal protein S4 |
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Authors: | I N Serdyuk J L Shpungin G Zaccai |
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Institution: | Institute of Protein Research Academy of Sciences of the U.S.S.R. Poustchino, Moscow Region, U.S.S.R.;Institut Laue-Langevin 156X Centre de Tri 38042 Grenoble, France |
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Abstract: | A fragment with a molecular weight of 170,000 and a sedimentation coefficient of 13 S which is capable of specifically binding ribosomal protein S4 has been obtained by digestion of Escherichia coli 16 S RNA with ribonuclease A. The 13 S fragment of 16 S RNA and its complex with protein S4 have been studied by different physical methods; in the first place, by neutron scattering. It has been shown that this fragment is very compact in solution. The radii of gyration of this fragment (50 ± 3 Å) and of protein S4 within the complex (17 ± 3 Å) coincide, within the limits of experimental error, with the radii of gyration for the free RNA fragment (47 ± 2 Å) and the free ribosomal protein S4 in solution (18 ± 2 Å). Hence the conclusion is drawn that the compactness of the RNA fragment and the ribosomal protein does not change on complex formation. The compact 13 S fragment of 16 S RNA is shown to be contrast-matched in solvent containing 70% 2H2O which corresponds to a value for the partial specific volume of RNA of 0.537 cm3/g. |
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