Interaction of Initiator Met-tRNAfMet (Escherichia coli) and Gly-tRNA1Gly (Staphylococcus epidermidis) with Bacterial Elongation Factor Tu: GTP Complex
- 1 April 1981
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 89 (5) , 1565-1572
- https://doi.org/10.1093/oxfordjournals.jbchem.a133350
Abstract
Jekowsky et al. reported recently that elongation factor Tu: GTP complex from Escherichia coli protected aminoacyl-tRNA from digestion by pancreatic RNase (1). On the basis of their finding, we have developed the “RNase-resistance assay” for determination of the dissociation constant of aminoacyl-tRNA from aminoacyl-tRNA: EF-Tu: GTP complex. By the use of this sensitive assay, the dissociation constants were estimated to be 3.6× 10−7M for Ala-tRNA1Ala (Torulopsis utilis), 7.9× 10−8 M for Phe-tRNAphe (Escherichia coli), 8.1 × 10-7 M for initiator Met-tRNAfMet (Escherichia coli), and 5.4 × 10-6 M for Gly-tRNA1Gly (Staphylococcus epidermidis) participating in cell wall biosynthesis. Moreover, using a relatively large amount of EF-Tu: GTP, we have been able to detect the ternary complexes of initiator Met-tRNAfMet and Gly-tRNAIGly with EF-Tu: GTP even by the method of gel filtration.This publication has 2 references indexed in Scilit:
- STUDIES ON POLYNUCLEOTIDES .81. YEAST PHENYLALANINE TRANSFER RIBONUCLEIC ACID - PARTIAL DIGESTION WITH PANCREATIC RIBONUCLEASE1968
- Purification of methionine-, valine-, phenylalanine- and tyrosine-specific tRNA from Escherichia coliBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1967