Abstract
As in the case with prokaryotic systems, Artemia salina elongation factors EF-1 and EF-2 interact with a common site or with closely overlapping sites on the Artemia ribosome. This feature of ribosomal design must restrict interaction with the ribosome to only one of the factors at alternating steps of chain elongation. In support of this view we find that EF-1, but not EF-2, interacts with the post-translocation ribosome, whereas the reverse is true of the pre-translocation ribosome. Conformational changes probably account for the alternating selectivity of the translating ribosome for each elongation factor.
MeSH Terms
Animals
Binding Sites
Carbon Radioisotopes
Decapoda
Guanosine Triphosphate/metabolism
Hydrolysis
Peptide Chain Elongation, Translational
Peptide Elongation Factors
Phenylalanine
Phosphorus Radioisotopes
Protein Conformation
RNA, Transfer/metabolism
Ribosomes/metabolism
Structure-Activity Relationship
Tritium
Chemicals
Carbon Radioisotopes
Peptide Elongation Factors
Phosphorus Radioisotopes
Tritium
Phenylalanine
Guanosine Triphosphate
RNA, Transfer
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Nombela C
Ochoa S
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