Abstract
Comparison of the known primary structures of several tRNAs reveals striking similarities between the nucleotide sequences of yeast tRNAphe and Escherichia coli tRNA1Val. On the assumption that such structural analogy might lead to aminoacylation of both tRNAs by each of the corresponding aminoacylâtRNA synthetases, a detailed study of this system was undertaken.The results indicate that under optimal conditions, E. coli tRNA1Val can be completely aminoacylated by yeast phenylalanylâtRNA synthetase, while the reciprocal (i.e. valylâtRNAPhe (yeast) formation by E. coli valylâtRNA synthetase) could not be demonstrated under any of a variety of conditions tested.Conditions for PheâtRNA1Val (E. coli) formation by yeast phenylalanylâtRNA synthetase differ radically from those leading to aminoacylation of tRNA in homologous systems. In particular, the final yield of aminoacylâtRNA varies with enzyme concentration and is markedly affected by the nature of the buffer and the pH, as well as by the presence of monovalent cations and organic solvents such as ethanol and dimethyl sulfoxide. Similar observations have already been reported in the study of the aminoacylation of tRNA in several heterologous systems.The results are discussed in relation to the structure of the two tRNAs.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
