Modification ofBacillus subtiliselongation factor Tu by N-tosyl-L phenylalanyl chloromethane abolishes its ability to interact with the 3′-terminal polynucleotide structure but not with the acyl bond in aminoacyl-tRNA-Reference-Cited by-同舟云学术

Modification ofBacillus subtiliselongation factor Tu by N-tosyl-L phenylalanyl chloromethane abolishes its ability to interact with the 3′-terminal polynucleotide structure but not with the acyl bond in aminoacyl-tRNA

Published:1989-07-17 Issue:1-2 Volume:251 Page:121-124
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Jonák Jiří,Karas Karel

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(89)81440-1/fullpdf

Reference16 articles.

1. Fluorescence of the Y base of yeast phenylalanine transfer ribonucleic acid. Effect of pH, aminoacylation, and interaction with elongation factor Tu

2. Ternary Complex Formation between Elongation Factor Tu, GTP and Aminoacyl-tRNA: an Equilibrium Study

3. Discrimination between aminoacyl groups on su+7 tRNA by elongation factor Tu

4. Interaction of Initiator Met-tRNAfMet (Escherichia coli) and Gly-tRNA1Gly (Staphylococcus epidermidis) with Bacterial Elongation Factor Tu: GTP Complex

5. Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Site-directed mutagenesis of elongation factor Tu. The functional and structural role of residue Cys81;European Journal of Biochemistry;1992-09

2. The influence of different modifications of elongation factor Tu fromEscherichia colion ternary complex formation investigated by fluorescence spectroscopy;Nucleic Acids Research;1990

3. Identification of the N -tosyl-L-phenylalanyl chloromethylketone modification site in Thermus thermophilus elongation factor Tu;FEBS Letters;1989-11-06