Abstract:
:In eukaryotic ribosome, the N domain of polypeptide release factor eRF1 is involved in decoding stop signals in mRNAs. However, structure of the decoding site remains obscure. Here, we specifically altered the stop codon recognition pattern of human eRF1 by point mutagenesis of the invariant Glu55 and Tyr125 residues in the N domain. The 3D structure of generated eRF1 mutants was not destabilized as demonstrated by calorimetric measurements and calculated free energy perturbations. In mutants, the UAG response was most profoundly and selectively affected. Surprisingly, Glu55Arg mutant completely retained its release activity. Substitution of the aromatic ring in position 125 reduced response toward all stop codons. This result demonstrates the critical importance of Tyr125 for maintenance of the intact structure of the eRF1 decoding site. The results also suggest that Tyr125 is implicated in recognition of the 3d stop codon position and probably forms an H-bond with Glu55. The data point to a pivotal role played by the YxCxxxF motif (positions 125-131) in purine discrimination of the stop codons. We speculate that eRF1 decoding site is formed by a 3D network of amino acids side chains.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Kolosov P,Frolova L,Seit-Nebi A,Dubovaya V,Kononenko A,Oparina N,Justesen J,Efimov A,Kisselev Ldoi
10.1093/nar/gki927keywords:
subject
Has Abstractpub_date
2005-11-10 00:00:00pages
6418-25issue
19eissn
0305-1048issn
1362-4962pii
33/19/6418journal_volume
33pub_type
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