Abstract
Bovine tryptophanyl-tRNA synthetase is able to form a complex with glyceraldehyde-3-phosphate dehydrogenase. The complex formation (i) does not influence the tryptophan-dependent PP i-ATP exchange reaction and (ii) involves predominantly the N-terminal dispensable domain of the synthetase. Glyceraldehyde-3-phosphate dehydrogenase was shown to be capable of interacting simultaneously with tryptophanyl-tRNA synthetase and with ribosomal RNA to form a ternary complex. It is proposed that compartmentation of some aminoacyl-tRNA synthetases in certain cases might be achieved via ‘adapter’ molecules which can bind at once to ribonucleic acids and to aminoacyl-tRNA synthetases.
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 callMore From: Biochemical and Biophysical Research Communications
Disclaimer: 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.
