Localization of surface peptide from ribosomal protein L7 on 80 S ribosome by biotinylation.
A surface topography of ribosomal peptides on ribosome particles was conducted by using N',Hydroxysuccinimido-biotin (NHS-biotin) modification. All rat ribosomal proteins, except proteins L3 and L8, are biotinylated when the ribosome particle is the substrate. A surface peptide from protein L7 was determined from biotinylated ribosomes by high performance liquid chromatography and cyanogen bromide peptide mapping. It was found that only the tandem repeats of the NH2-terminal segment of protein L7 are accessible to biotinylation. It is concluded that the NH2-terminal-end of protein L7 should be exposed on the surface of ribosomal particles.
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Institute of Genetics, National Yang-Ming Medical College, Taipei, Taiwan, Republic of China.
D000818:Animals; D001710:Biotin / Q000031:analogs & derivatives*; D002851:Chromatography, High Pressure Liquid; D003488:Cyanogen Bromide; D004591:Electrophoresis, Polyacrylamide Gel; D007202:Indicators and Reagents; D008099:Liver / Q000648:ultrastructure; D010449:Peptide Mapping; D051381:Rats; D012269:Ribosomal Proteins / Q000032:analysis*; D012270:Ribosomes / Q000737:chemistry*; D013388:Succinimides
D007202:Indicators and Reagents; D012269:Ribosomal Proteins; D013388:Succinimides; C033788:biotinyl N-hydroxysuccinimide ester; D001710:Biotin; D003488:Cyanogen Bromide