Replacement of L7/L12.L10 Protein Complex in Escherichia coli Ribosomes with the Eukaryotic Counterpart Changes the Specificity of Elongation Factor Binding
Open Access
- 1 September 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (39) , 27578-27582
- https://doi.org/10.1074/jbc.274.39.27578
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosomeNature, 1997
- Cooperative Interactions of RNA and Thiostrepton Antibiotic with Two Domains of Ribosomal Protein L11Biochemistry, 1996
- Structure and evolution of mammalian ribosomal proteinsBiochemistry and Cell Biology, 1995
- Ribosomal Proteins L11 and L10.(L12)4 and the Antibiotic Thiostrepton Interact with Overlapping Regions of the 23 S rRNA Backbone in the Ribosomal GTPase CentreJournal of Molecular Biology, 1993
- Characterization of the binding sites of protein L11 and the L10.(L12)4 pentameric complex in the GTPase domain of 23 S ribosomal RNA from Escherichia coliJournal of Molecular Biology, 1990
- Ribosomal proteins of Escherichia coli localization and possible molecular mechanism in translationJournal of Molecular Biology, 1983
- The role of guanosine 5′-triphosphate in polypeptide chain elongationBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978
- Interchangeability of elongation factor-Tu and elongation factor-1 in aminoacyl-tRNA binding to 70 S and 80 S ribosomesFEBS Letters, 1977
- The ribosomal protein L8 is a complex of L7/L12 and L10FEBS Letters, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970