The binding of ribosomal protein S4 does not change the gross conformation of the 16 S RNA.
The binding of ribosomal protein S4 to the 16 S RNA does not result in a large shape or conformational change in the 16 S RNA under the conditions of reconstitution. The sedimentation coefficient, frictional coefficient ratio, and effective hydrodynamic radius of the 16 S RNA.protein S4 complex are very similar to those obtained for the 16 S RNA free in solution. Only subtle conformational differences were obtained in the comparison of the complex and free 16 S RNA by circular dichroism. Thus, extensive organization of the 16 S RNA by ribosomal protein S4 is not a step in the process of self-assembly of the 30 S subunit.
D002942:Circular Dichroism; D046911:Macromolecular Substances; D009690:Nucleic Acid Conformation / Q000187:drug effects*; D011485:Protein Binding; D012313:RNA / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D014461:Ultracentrifugation
D046911:Macromolecular Substances; D012269:Ribosomal Proteins; D012313:RNA