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Localization of surface peptide from ribosomal protein L7 on 80 S ribosome by biotinylation
Author(s) -
Lin Alan
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80030-7
Subject(s) - biotinylation , ribosome , peptide , ribosomal rna , ribosomal protein , chemistry , eukaryotic ribosome , biochemistry , microbiology and biotechnology , biology , rna , gene
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 NH 2 ‐terminal segment of protein L7 are accessible to biotinylation. It is concluded that the NH 2 ‐terminal‐end of protein L7 should be exposed on the surface of ribosomal particles.