Initiator-like properties of a methionyl-tRNA from wheat embryos
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The two major methionyl-tRNA species from wheat embryos and E. coli have been studied as regards their capacity to form a ternary complex with GTP and the ribosomal binding enzyme from both sources. Methionyl-tRNA1 from wheat resembles met-tRNAF from E. coli in its inability to interact with the homologous enzyme. It also fails to complex with the bacterial enzyme. Methionyl-tRNA2 from wheat is similar to met-tRNAM from E. coli in that forms the ternary complex with the enzyme from both organisms. Wheat met-tRNA1 has a markedly higher affinity for binding "non-enzymatically" to wheat ribosomes in the presence of ApUpG than does met-tRNA2. © 1970.
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