Localization of ribosomal protein L27 at the peptidyl transferase centre of the 50 S subunit, as determined by immuno-electron microscopy
- 1 December 1987
- journal article
- research article
- Published by Springer Nature in Molecular Genetics and Genomics
- Vol. 210 (3) , 498-503
- https://doi.org/10.1007/bf00327203
Abstract
Protein L27 has been localized on the ribosomal surface by immuno-electron microscopy by using antibodies specific for Escherichia coli L27, and by reconstituting 50 S subunits from an E. coli mutant, which lacks protein L27, with the homologous protein from Bacillus subtilis and using antibodies specific for the B. subtilis protein. With both approaches, protein L27 has been located at the base of the central protuberance at the interface side of the 50 S particle and thus in proximity to the peptidyl transferase centre. The immuno-electron microscopic data also suggest that the interface region of the 50 S particle is not as flat as most of the proposed three-dimensional models suggest, but instead there is a significant depression.Keywords
This publication has 43 references indexed in Scilit:
- A mutant from Escherichia coli which lacks ribosomal proteins S17 and L29 used to localize these two proteins on the ribosomal surfaceEuropean Journal of Biochemistry, 1985
- Immunoelectron Microscopy of RibosomesAnnual Review of Biophysics and Bioengineering, 1984
- Immunoelectron microscopy of ribosomes carrying a fluorescence label in a defined positionFEBS Letters, 1983
- Ribosomal proteins L1, L17 and L27 from Escherichia coli localized at single sites on the large subunit by immune electron microscopyJournal of Molecular Biology, 1981
- Mutants of Escherichia coli lacking ribosomal protein L1Journal of Molecular Biology, 1981
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- The mechanism of covalent reaction of bromoacetyl-phenylalanyl-transfer RNA with the peptidyl-transfer RNA binding site of the Escherichia coli ribosomeJournal of Molecular Biology, 1974
- Identification of a protein at the ribosomal donor-site by affinity labelingBiochemical and Biophysical Research Communications, 1974
- Protein a from Staphylococcus aureus. Its isolation by affinity chromatography and its use as an immunosorbent for isolation of immunoglobulinsFEBS Letters, 1972
- Ribosomal proteins. XXV. Immunological studies on Escherichia coli ribosomal proteinsJournal of Molecular Biology, 1971