Physical characteristics of the reconstitution intermediates (RI30 and RI30*) from the 30S ribosomal subunit of Escherichia coli.
The isolated reconstitution intermediates (RI30 and RI30*) from the 30S ribosomal subunit of Escherichia coli were found to contain ten proteins. The sedimentation coefficients, diffusion coefficients, density increments, extinction coefficients, and molecular weights were determined for the reconstitution particles and compared with those obtained from the 16S rRNA under identical buffer conditions. The results show that the binding of the proteins on the 16S rRNA at 4 degrees C does not markedly affect the folding of the RNA molecule. However, upon heating the RI30 particle at 40 degrees C to form the RI30* particle, significant folding of the RNA took place, giving a structure considerably more compact than that of the 16S rRNA or the RI30 particle.
D004926:Escherichia coli / Q000378:metabolism / Q000648:ultrastructure*; D014176:Protein Biosynthesis; D012335:RNA, Ribosomal / Q000378:metabolism; D012269:Ribosomal Proteins / Q000302:isolation & purification* / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism / Q000648:ultrastructure*
D012335:RNA, Ribosomal; D012269:Ribosomal Proteins