A neutron investigation of yeast valyl-tRNA synthetase interaction with tRNAs.
A new way of studying RNA-protein complexes, using neutron small angle scattering in solution, is described and was applied in the case of the system, yeast valyl-tRNA synthetase, interacting with its cognate and non cognate yeast tRNAs. It was shown that, when limited amounts of tRNA (either cognate or non cognate) are added to valyl-tRNA synthetase, a complex consisting of two enzyme molecules and one tRNA molecule is first formed. It is subsequently dissociated to a one to one complex when more tRNA is present in the solution. The association curve shows a maximum for a molecular ratio, enzyme over tRNA, equal to 2.
D000604:Amino Acyl-tRNA Synthetases; D001224:Aspartic Acid; D007700:Kinetics; D009239:N-Formylmethionine; D009502:Neutrons; D011485:Protein Binding; D012343:RNA, Transfer; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012542:Scattering, Radiation; D014633:Valine; D014637:Valine-tRNA Ligase
D001224:Aspartic Acid; D009239:N-Formylmethionine; D012343:RNA, Transfer; D000604:Amino Acyl-tRNA Synthetases; D014637:Valine-tRNA Ligase; D014633:Valine