Abstract
The affinity of ribosomes for the elongation factors EF1 and EF2 changes while the ribosome is going through the different steps of the elongation cycle. In this communication we provide evidence that the affinity of the EF1-aa-tRNA-GTP complex for the ribosomal acceptor site differs for ribosomes having their donor site either vacant or occupied by peptidyl-tRNA or by uncharged tRNA. Ribosomes having peptidyl-tRNA at their donor site bind the EF1 complex with the highest affinity.
Results are discussed in light of recent findings that the two elongation factors are not bound to the ribosome simultaneously.
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Baksht, E., De Groot, N. The enzymatic binding of aminoacyl-tRNA to reticulocyte ribosomes: The stimulatory effect of donor site bound peptidyl-tRNA. Molecular Biology Reports 1, 493–497 (1974). https://doi.org/10.1007/BF00360677
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DOI: https://doi.org/10.1007/BF00360677