Structural differences between active and inactive mammalian 60S ribosomal subunits. Circular dichroism and electric birefringence studies.
The structure and conformation of different active and inactive forms of the 60S rat liver ribosomal subunits have been analyzed by electric birefringence and circular dichroism. These studies show the following: 1) When a phosphate buffer is used instead of a triethanolamine buffer, there are major changes in RNA stacking, RNA-protein interactions, and particle orientation and conformation with no concomitant loss in ribosome activity. 2) The inactivated subunits by K(+)-depletion exhibit the same electro-optical and near-UV CD behaviour than the active subunits in phosphate buffer. 3) Inactivation by EDTA-treatment leads to drastic changes in RNA structure, RNA-protein interactions and subunit conformation; the 60S particles behave like free RNA, indicating the absence of any stabilization of rRNA by ribosomal proteins. 4) The inactivation of subunits by depletion of either monovalent or divalent cations is accompanied by a net decrease of the alpha-helicity of the ribosomal proteins. 5) The transition from active to inactive form of 60S subunits may involve protein modifications, likely dependent on a specific array of cations. 6) RNA has a certain degree of liberty within the subunits and one can suppose that this property is responsible for the flexible structure of ribosome.
Marion
M J
MJ
Laboratoire de Biologie et Technologie des Membranes, C.N.R.S. UMR 9, Université Claude Bernard de Lyon, Villeurbanne, France.
Marion
C
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D000818:Animals; D001718:Birefringence; D002942:Circular Dichroism; D006358:Hot Temperature; D008297:Male; D008968:Molecular Conformation; D009691:Nucleic Acid Denaturation; D010449:Peptide Mapping; D011489:Protein Denaturation; D051381:Rats; D011919:Rats, Inbred Strains; D012269:Ribosomal Proteins / Q000032:analysis; D012270:Ribosomes / Q000032:analysis; D013816:Thermodynamics
D012269:Ribosomal Proteins