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Titolo:
Class-1 polypeptide chain release factors are structurally and functionally similar to suppressor tRNAs and comprise different structural-functional families of prokaryotic/mitochondrial and eukaryotic/archaebacterial factors
Autore:
Kisselev, LL; Oparina, NY; Frolova, LY;
Indirizzi:
Russian Acad Sci, Engelhardt Inst Mol Biol, Moscow 117984, Russia Russian Acad Sci Moscow Russia 117984 st Mol Biol, Moscow 117984, Russia
Titolo Testata:
MOLECULAR BIOLOGY
fascicolo: 3, volume: 34, anno: 2000,
pagine: 363 - 377
SICI:
0026-8933(200005/06)34:3<363:CPCRFA>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSFER-RNA SYNTHETASE; ELONGATION-FACTOR-G; ESCHERICHIA-COLI; TRANSLATION TERMINATION; CRYSTAL-STRUCTURE; MESSENGER-RNA; FISSION YEAST; GENETIC-CODE; FACTORS ERF1; AMINO-ACIDS;
Keywords:
translation termination; release factors; eRF1; aRF1; RF1; RF2; mtRF; eukaryotes; archaebacteria; prokaryotes; domain structure; primary structure; suppressor tRNA; protein biosynthesis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Kisselev, LL Russian Acad Sci, Engelhardt Inst Mol Biol, Moscow 117984, Russia Russian Acad Sci Moscow Russia 117984 Moscow 117984, Russia
Citazione:
L.L. Kisselev et al., "Class-1 polypeptide chain release factors are structurally and functionally similar to suppressor tRNAs and comprise different structural-functional families of prokaryotic/mitochondrial and eukaryotic/archaebacterial factors", MOL BIOL, 34(3), 2000, pp. 363-377

Abstract

Class-1 polypeptide chain release factors (RF) induce peptidyl-tRNA hydrolysis in the ribosome if any of the three stop codons encounters the ribosomal A site. We have shown earlier that all factors of this class possess a common functionally essential motif GGQ. In this study we analyzed the primary structures of all known class-1 factors taken from the data banks together with the experimental data available on their structural and functional organization. The following conclusions were drawn. 1.Amino acid sequences of eukaryotic and archaebacterial factors (eRF1 and aRF1, respectively) show high similarity. This suggests the potential ability of eRF1 to function in archaebacterial and aRF1 in eukaryotic ribosomes, and points to their origin from a common ancestor. 2. Primary structures of class-1 release factors from prokaryotes and eukaryotic mitochondria show no statistically significant similarity with archaebacterial and cytoplasmic eukaryotic release factors, except for a common motif GGQ. This confirms our earlier conclusion(Nature, 1994, vol. 372, pp. 701-703) and contradicts the hypothesis of Ito et al. (Proc. Natl. Acad. Sci. USA, 1996, vol. 93, pp. 5443-5448) about structural similarity of all class-1 release factors. 3. All the eRF1/aRF1 recognizing three stop codons have a common motif NIKs that is absent from eubacterial RFI and RF2, each of which is able to recognize two stop codons of the three. We suppose that the function of the NIKs motif is to fix the proper orientation of eRF1/aRF1 at the ribosome. 4. The domain structure and functional properties of eRF1/aRF1 point to the similarity of these factors with suppressor tRNAs as suggested long ago, and also semblance with aminoacyl-tRNA synthetases. 5. Considering that peptidyl-tRNA is fixed at the ribosomal P site while the stop codon and termination factor are at the A site, it may be presumed that the distance between the functionally essential motifs NIKs and GGQS in eRF1/aRF1 should approximately correspond to the distance between the anticodon and the aminoacyl end of aminoacyl-tRNA located at the ribosomal A site.

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Documento generato il 09/04/20 alle ore 19:40:59