Ontology highlight
ABSTRACT:
SUBMITTER: Kolosov P
PROVIDER: S-EPMC1283522 | biostudies-literature | 2005
REPOSITORIES: biostudies-literature
Kolosov Petr P Frolova Ludmila L Seit-Nebi Alim A Dubovaya Vera V Kononenko Artem A Oparina Nina N Justesen Just J Efimov Alexandr A Kisselev Lev L
Nucleic acids research 20051110 19
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, t ...[more]