Class-1 translation termination factors: Invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition

Nucleic Acids Research

Volumn 29, Issue 19, 2001, Pages 3982-3987

  Seit Nebi, Alim ^a   Frolova, Ludmila ^a,b   Justesen, Just ^b   Kisselev, Lev ^a  

^a ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^b AARHUS UNIVERSITY   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; ARGININE; ESTER; GLUTAMINE; GLYCINE; ISOLEUCINE; PEPTIDE; PEPTIDYLTRANSFERASE; RIBOSOME RNA; TRANSFER RNA; TRANSLATION TERMINATION FACTOR; WATER;

AMINO ACID SUBSTITUTION; ARTICLE; CONFORMATION; CONTROLLED STUDY; HUMAN; HYDROLYSIS; MOLECULAR RECOGNITION; MUTANT; PRIORITY JOURNAL; PROTEIN MOTIF; RIBOSOME; SITE DIRECTED MUTAGENESIS; STOP CODON;

EID: 0035476654     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/29.19.3982     Document Type: Article

References (30)

1. Translational termination comes of age
2. A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor
3. Mimicry grasps reality in translation termination
4. Direct recognition of mRNA stop signals by Escherichia coli polypeptide chain release factor two
5. Decoding the translational termination signal: The polypeptide chain release factor in Escherichia coli crosslinks to the base following the stop codon
6. The polypeptide chain release factor eRF1 specifically contacts the sUGA stop codon located in the A site of eukaryotic ribosomes
7. Terminating eukaryote translation: Domain 1 of release factor eRF1 functions in stop codon recognition
8. A tripeptide anticodon deciphers stop codons in messenger RNA
9. Ribosomal RNAs in translation termination: Facts and hypotheses
10. Class 1 translation termination factors are structurally and functionally similar to suppressor tRNA and are related to various structural-functional families (prokaryotes and mitochondria-eukaryotes and archaebacteria)
11. Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
12. The crystal structure of human eukaryotic release factors eRF1 - Mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
13. Translation termination in eukaryotes: Polypeptide release factor eRF1 is composed of functionally and structurally distinct domains
14. Identification of a human cDNA with high homology to yeast omnipotent suppressor 45
15. Functional expression of eukaryotic polypeptide chain release factors 1 and 3 by means of baculovirus/insect cells and complex formation between the factors
16. A human homologue of the yeast GST1 gene codes for a GTP-binding protein and is expressed in a proliferation-dependent manner in mammalian cells
17. Mammalian release factor: In vitro assay and purification
18. Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome-dependent guanosine triphosphatase
19. Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3
20. The ciliate Euplotes octocarinatus expresses two polypeptide release factors of the type eRF1
21. Class I release factors in ciliates with variant genetic codes
22. The molecular basis of nuclear genetic code change in ciliates
23. Stop codon recognition in ciliates: Euplotes release factor does not respond to reassigned UGA codon
24. The structural basis of ribosome activity in peptide bond synthesis
25. Protein-RNA interactions: A structural analysis
26. Recent advances in RNA-protein recognition
27. A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation
28. Functional specificity of amino acid at position 246 in the tRNA mimicry domain of bacterial release factor 2
29. Genetic probes to bacterial release factors: tRNA mimicry hypothesis and beyond
30. The ribosomal binding and peptidyl-tRNA hydrolysis functions of Escherichia coli release factor 2 are linked through residue 246