Chemical basis for heterogeneity of ribosomal proteins.
- 1 April 1968
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 59 (4), 1329-1336
- https://doi.org/10.1073/pnas.59.4.1329
Abstract
Amino-acid compositions are given for 14 of the 15 individual proteins isolated from the SOS ribosome of Escherichia coli. Each protein is unique and none is formed by the dimerization of any 2 of the others. At least 15 cistrons control the structure of the proteins of the 30S ribosome.Keywords
This publication has 13 references indexed in Scilit:
- Primary Structure Heterogeneity in Ribosomal Proteins from Escherichia coliNature, 1967
- Ribosomal proteins of Escherichia coli. I. Demonstration of different primary structures.Proceedings of the National Academy of Sciences, 1967
- Mammalian Ribosomal Protein: Analysis by Electrophoresis on Polyacrylamide GelScience, 1967
- Physical and functional heterogeneity of ribosomal proteinsJournal of Molecular Biology, 1966
- The requirements for specific sRNA binding by ribosomesJournal of Molecular Biology, 1966
- In vitro recovery of ribosomes and of synthetic activity from synthetically inactive ribosomal subunitsJournal of Molecular Biology, 1966
- Isolation and characterization of ribonuclease I mutants of Escherichia coliJournal of Molecular Biology, 1966
- Reconstitution of functionally active ribosomes from inactive subparticles and proteins.Proceedings of the National Academy of Sciences, 1966
- Fractionation of the ribosomal protein from Escherichia coliJournal of Molecular Biology, 1964
- STUDIES ON THE COMPOSITION OF THE PROTEIN FROM ESCHERICHIA COLI RIBOSOMESProceedings of the National Academy of Sciences, 1961