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YearIMPACT-FACTOR
2022  1,200
2021  1,540
2020  1,374
2019  1,023
2018  0,932
2017  0,977
2016  0,799
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2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 42(2008) N 6 p. 939-948;
E.V. Ivanova1, E.Z. Alkalaeva1,2, B. Birdsall3, P.M. Kolosov1, V.I. Polshakov4, L.L. Kisselev1

Interface of the interaction of the middle domain of human translation termination factor eRF1 with eukaryotic ribosomes

1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991, Russia
2University of Oslo, Center of Medical Research, Moscow, 119991, Russia
3Molecular Structure Division, National Institute for Medical Research, Mill Hill, London, NW71AA, UK
4Center of Magnetic Tomography and Spectroscopy, Moscow State University, Moscow, 119991, Russia
Received - 2008-06-18; Accepted - 2008-07-01

Translation termination in eukaryotes is governed by the interaction of two, class 1 and class 2, polypeptide chain release factors with the ribosome. The middle (M) domain of the class 1 factor eRF1 contains the strictly conserved GGQ motif and is involved in hydrolysis of the peptidyl-tRNA ester bond in the peptidyl transferase center of the large ribosome subunit. Heteronuclear NMR spectroscopy was used to map the interaction interface of the M domain of human eRF1 with eukaryotic ribosomes. The protein was found to specifically interact with the 60S subunit, since no interaction was detected with the 40S subunit. The amino acid residues forming the interface mostly belong to long helix α1 of the M domain. Some residues adjacent to α1 and belonging to strand β5 and short helices α2 and α3 are also involved in the protein-ribosome contact. The functionally inactive G183A mutant interacted with the ribosome far more weakly as compared with the wild-type eRF1. The interaction interfaces of the two proteins were nonidentical. It was concluded that long helix α1 is functionally important and that the conformational flexibility of the GGQ loop is essential for the tight protein-ribosome contact.

eukaryotic ribosome, middle domain of eRF1, translation termination, NMR spectroscopy, protein-ribosome interaction



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