Mobile domains in ribosomes revealed by proton nuclear magnetic resonance.
Ribosomes and subunits from eukaryotic and prokaryotic sources were studied by high-resolution proton magnetic-resonance spectroscopy. If all ribosomal components are firmly bound within the particle, then only broad spectra would be expected. However, relatively sharp resonances were found both in ribosomal subunits and in 70 or 80 S ribosomes. The regions of these mobile protein domains have been partially assigned in Escherichia coli ribosomes. Large and small ribosomal subunits were treated to remove selectively proteins L7/12 and S1, respectively. Sharp proton magnetic resonance spectra were not observed for the stripped large subunit showing that proteins L7/12 comprise the flexible protein region and that there is little other flexibility in the stripped subunit. Complete removal of S1 from the small subunit greatly reduced but did not abolish the sharp protein resonance peaks, indicating that protein S1 contains a substantial flexible component but that other flexible components remain in the stripped small subunit. Evidence for generality of these features of ribosome organization is provided by similar studies on ribosomes from eukaryotic sources.
D000818:Animals; D001156:Artemia; D002499:Centrifugation, Density Gradient; D004926:Escherichia coli / Q000648:ultrastructure; D008099:Liver / Q000648:ultrastructure; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011817:Rabbits; D051381:Rats; D012156:Reticulocytes / Q000648:ultrastructure; D012269:Ribosomal Proteins / Q000032:analysis; D012270:Ribosomes / Q000648:ultrastructure*; D012441:Saccharomyces cerevisiae / Q000648:ultrastructure; D013045:Species Specificity
D012269:Ribosomal Proteins