A single proteolytic cleavage in release factor 2 stabilizes ribosome binding and abolishes peptidyl-tRNA hydrolysis activity.
Open Access
- 1 July 1994
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 269 (29) , 18899-18903
- https://doi.org/10.1016/s0021-9258(17)32252-4
Abstract
No abstract availableThis publication has 21 references indexed in Scilit:
- Solution of the ribosome riddle: how the ribosome selects the correct aminoacyl‐tRNA out of 41 similar contestantsMolecular Microbiology, 1993
- A compilation of large subunit (23S and 23S-like) ribosomal RNA structures: 1993Nucleic Acids Research, 1993
- Functional domains in the Escherichia coli release factorsEuropean Journal of Biochemistry, 1993
- Release Factor-dependent False Stops are Infrequent in Escherichia coliJournal of Molecular Biology, 1993
- Two regions of theEscherichia cqli16S ribosomal RNA are important for decoding stop signals in polypeptide chain terminationNucleic Acids Research, 1993
- Recoding: Reprogrammed Genetic DecodingScience, 1992
- Site-Specific Incorporation of Novel Backbone Structures into ProteinsScience, 1992
- Interaction of the release factors with the Escherichia coli ribosome: structurally and functionally-important domainsBiochimie, 1991
- Hydrolysis of fMet-tRNA by Peptidyl TransferaseProceedings of the National Academy of Sciences, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970