Abstract
Class‐1 translation termination factors (release factors (RFs)) from Eukarya (eRF1) and Archaea (aRF1) exhibit a high degree of amino acid sequence homology and share many common motifs. In contrast to eRF1, function(s) of aRF1 have not yet been studied in vitro. Here, we describe for the first time the cloning and expression in Escherichia coli of the gene encoding the peptide chain RF from the hyperthermophilic archaeon Methanococcus jannaschii (MjaRF1). In an in vitro assay with mammalian ribosomes, MjaRF1, which was overproduced in E. coli, was active as a RF with all three termination codon‐containing tetraplets, demonstrating the functional resemblance of aRF1 and eRF1. This observation confirms the earlier prediction that eRF1 and aRF1 form a common structural–functional eRF1/aRF1 protein family, originating from a common ancient ancestor.
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Dates
Type | When |
---|---|
Created | 23 years ago (July 25, 2002, 10:30 p.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 11:35 p.m.) |
Indexed | 1 month, 1 week ago (July 11, 2025, 6:15 a.m.) |
Issued | 25 years, 3 months ago (April 27, 2000) |
Published | 25 years, 3 months ago (April 27, 2000) |
Published Online | 25 years, 3 months ago (April 27, 2000) |
Published Print | 25 years, 3 months ago (April 28, 2000) |
@article{Dontsova_2000, title={Translation termination factor aRF1 from the archaeon Methanococcus jannaschii is active with eukaryotic ribosomes}, volume={472}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(00)01466-6}, DOI={10.1016/s0014-5793(00)01466-6}, number={2–3}, journal={FEBS Letters}, publisher={Wiley}, author={Dontsova, Maria and Frolova, Ludmila and Vassilieva, Julia and Piendl, Wolfgang and Kisselev, Lev and Garber, Maria}, year={2000}, month=apr, pages={213–216} }