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Small-Angle X-Ray Studies on the Structure of 16-S Ribosomal RNA and of a Complex of Ribosomal Protein S4 and 16-S Ribosomal RNA from <em>Escherichia coli</em>.

Authors :
Folkhard, Waltraud
Pilz, Ingrid
Kratky, Otto
Garrett, Roger
Stöffler, Georg
Source :
European Journal of Biochemistry; Nov75 Part 1, Vol. 59 Issue 1, p63-71, 9p
Publication Year :
1975

Abstract

16-S ribosomal RNA and a complex of ribosomal protein S4 and 16-S rRNA were studied in solution by small-angle X-ray scattering. Concentration series of the 16-S rRNA and the S4 &#183; 16-S-rRNA complex were measured in 37.5 mM Tris-HCl buffer pH 7.4 at 5&#176;C. The following data were determined. The radii of gyration for the 16-S rRNA and S4 &#183; 16S-rRNA complex were R = 17.6 &#177; 0.4 nm and 17.5 &#177; 0.6 nm, respectively. The two respective values of the radii of gyration of the cross-section were R&lt;subscript&gt;q.1&lt;/subscript&gt; = 8.42 &#177; 0.1 nm and 8.33 &#177; 0.3 nm, and R&lt;subscript&gt;q.2&lt;/subscript&gt; = 0.988 &#177; 0.03 nm and 0.996 &#177; 0.03 nm. The largest diameters of the 16-S RNA and S4 &#183; 16-S-RNA complex were L = 61.8 &#177; 1 nm and 60.0 &#177; 1 nm, respectively. Volumes of V = 1570 &#177; 60 nm&#179; were found for both particles. In the Tris buffer used, no significant differences were found between the scattering curves of 16-S rRNA and the S4 &#183; 16-S-rRNA complex. A model equivalent in scattering properties to the RNA and complex is a flat elliptical cylinder with the following dimensions: large axis 61.7 nm, small axis 35.4 nm and height 2 nm. The theoretical scattering curve fits the experimental one as long as the shape of the measured curve is due to the overall shape of the particle. A model equivalent in scattering over the whole measured angular range is one built up from a large numbe of spheres that simulate the known substructure of the RNA. The outer dimensions of this model correspond to those of the flat elliptical cylinder. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00142956
Volume :
59
Issue :
1
Database :
Complementary Index
Journal :
European Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
15807180
Full Text :
https://doi.org/10.1111/j.1432-1033.1975.tb02425.x