Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.
Open Access
- 1 April 1984
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (8) , 5010-5016
- https://doi.org/10.1016/s0021-9258(17)42947-4
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- The elongation factor Tu binds aminoacyl-tRNA in the presence of GDP.Journal of Biological Chemistry, 1982
- Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor TuBiochemistry, 1981
- Interaction of Initiator Met-tRNAfMet (Escherichia coli) and Gly-tRNA1Gly (Staphylococcus epidermidis) with Bacterial Elongation Factor Tu: GTP ComplexThe Journal of Biochemistry, 1981
- The role of guanosine 5′-triphosphate in polypeptide chain elongationBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978
- Mechanisms in Polypeptide Chain Elongation on RibosomesProgress in Nucleic Acid Research and Molecular Biology, 1978
- Specificity of Elongation Factor Tu from Escherichia coli with Respect to Attachment of the Amino Acid to the 2' or 3'-Hydroxyl Group of the Terminal Adenosine of tRNAEuropean Journal of Biochemistry, 1977
- Isolation, characterization and structural implications of a nuclease-digested complex of aminoacyl transfer RNA and Escherichia coli elongation factor TuJournal of Molecular Biology, 1977
- Interaction of elongation factor Tu with 2'(3')-O-aminoacyloligonucleotides derived from the 3' terminus of aminoacyl-tRNA.Proceedings of the National Academy of Sciences, 1975
- Effect of the presence of a pCpCpCA 3′‐terminus in Phe‐tRNAPheyeast on the interaction with elongation factors and with the poly U‐ribosome systemFEBS Letters, 1972
- Inactivation of Tu Factor-Guanosine Triphosphate Recognition and Ribosome-binding Ability by Terminal Oxidation-Reduction of Yeast Phenylalanine Transfer Ribonucleic AcidPublished by Elsevier ,1972