scholarly journals Two-step model of stop codon recognition by eukaryotic release factor eRF1

2013 ◽  
Vol 41 (8) ◽  
pp. 4573-4586 ◽  
Author(s):  
Polina Kryuchkova ◽  
Alexander Grishin ◽  
Boris Eliseev ◽  
Anna Karyagina ◽  
Ludmila Frolova ◽  
...  
Keyword(s):  
Stop Codon ◽  
Release Factor ◽  
Codon Recognition ◽  
Step Model ◽  
Stop Codon Recognition

scholarly journals Eukaryotic Release Factor 1 Phosphorylation by CK2 Protein Kinase Is Dynamic but Has Little Effect on the Efficiency of Translation Termination in Saccharomyces cerevisiae

2006 ◽  
Vol 5 (8) ◽  
pp. 1378-1387 ◽  
Author(s):  
Adam K. Kallmeyer ◽  
Kim M. Keeling ◽  
David M. Bedwell
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Synthesis ◽  
Protein Kinase ◽  
Stop Codon ◽  
Translation Termination ◽  
Release Factor ◽  
Codon Recognition ◽  
Number Of Factors ◽  
Stop Codon Recognition

ABSTRACT Protein synthesis requires a large commitment of cellular resources and is highly regulated. Previous studies have shown that a number of factors that mediate the initiation and elongation steps of translation are regulated by phosphorylation. In this report, we show that a factor involved in the termination step of protein synthesis is also subject to phosphorylation. Our results indicate that eukaryotic release factor 1 (eRF1) is phosphorylated in vivo at serine 421 and serine 432 by the CK2 protein kinase (previously casein kinase II) in the budding yeast Saccharomyces cerevisiae. Phosphorylation of eRF1 has little effect on the efficiency of stop codon recognition or nonsense-mediated mRNA decay. Also, phosphorylation is not required for eRF1 binding to the other translation termination factor, eRF3. In addition, we provide evidence that the putative phosphatase Sal6p does not dephosphorylate eRF1 and that the state of eRF1 phosphorylation does not influence the allosuppressor phenotype associated with a sal6Δ mutation. Finally, we show that phosphorylation of eRF1 is a dynamic process that is dependent upon carbon source availability. Since many other proteins involved in protein synthesis have a CK2 protein kinase motif near their extreme C termini, we propose that this represents a common regulatory mechanism that is shared by factors involved in all three stages of protein synthesis.

scholarly journals PABP enhances release factor recruitment and stop codon recognition during translation termination

2016 ◽  
Vol 44 (16) ◽  
pp. 7766-7776 ◽  
Author(s):  
Alexandr Ivanov ◽  
Tatyana Mikhailova ◽  
Boris Eliseev ◽  
Lahari Yeramala ◽  
Elizaveta Sokolova ◽  
...  
Keyword(s):  
Stop Codon ◽  
Translation Termination ◽  
Release Factor ◽  
Codon Recognition ◽  
Stop Codon Recognition

scholarly journals Kinetics of Stop Codon Recognition by Release Factor 1

Biochemistry ◽  
2009 ◽  
Vol 48 (47) ◽  
pp. 11178-11184 ◽  
Author(s):  
Byron Hetrick ◽  
Kristin Lee ◽  
Simpson Joseph
Keyword(s):  
Stop Codon ◽  
Release Factor ◽  
Codon Recognition ◽  
Stop Codon Recognition ◽  
Kinetics Of

Functional characterization of polypeptide release factor 1b in the ciliate Euplotes

2010 ◽  
Vol 30 (6) ◽  
pp. 425-431 ◽  
Author(s):  
Yan Wang ◽  
Baofeng Chai ◽  
Wei Wang ◽  
Aihua Liang
Keyword(s):  
Stop Codon ◽  
Functional Characterization ◽  
Subcellular Location ◽  
Class I ◽  
Release Factor ◽  
Amino Acid Motif ◽  
Codon Recognition ◽  
Stop Codon Recognition ◽  
Higher Eukaryotes

In higher eukaryotes, RF-I (class I release factor) [eRF1 (eukaryotic release factor 1)] is responsible for stop codon recognition and promotes nascent polypeptide release from the ribosome. Interestingly, two class I RFs, eRF1a and eRF1b, have been identified among the ciliates Euplotes, which are variant code organisms. In the present study, we analysed the comparative expression of eRF1a and eRF1b in Euplotes cells, demonstrating that the expression of eRF1b was higher than that of eRF1a. An interaction between eRF1b and eRF3 was confirmed, suggesting that an eRF1b function is facilitated by eRF3. Co-localization of both eRF1s indicated that they function in the same subcellular location in Euplotes cells. We also analysed the characteristics of stop codon discrimination by eRF1b. Like eRF1a, eRF1b recognized UAA and UAG as stop codons, but not UGA. This finding disagreed with the deduced characteristics of eRF1a/eRF1b from the classic hypothesis of ‘anticodon-mimicry’ proposed by Muramatsu et al. [Muramatsu, Heckmann, Kitanaka and Kuchino (2001) FEBS Lett. 488, 105–109]. Mutagenesis experiments indicated that the absolutely conserved amino acid motif ‘G31T32’ (numbered as for human eRF1) in eRF1b was the key to efficient stop codon recognition by eRF1b. In conclusion, these findings support and improve the ‘cavity model’ of stop codon discrimination by eRF1 proposed by Bertram et al. [Bertram, Bell, Ritchie, Fullerton and Stansfield (2000) RNA 6, 1236–1247] and Inagaki et al. [Inagaki, Blouin, Doolittle and Roger (2002) Nucleic Acids Res. 30, 532–544].

Identification of amino acids responsible for stop codon recognition for polypeptide chain release factor

2013 ◽  
Vol 91 (3) ◽  
pp. 155-164 ◽  
Author(s):  
Lijun Xu ◽  
Yanrong Hao ◽  
Cui Li ◽  
Quan Shen ◽  
Baofeng Chai ◽  
...  
Keyword(s):  
Stop Codon ◽  
Translation Termination ◽  
Release Factor ◽  
Codon Reassignment ◽  
Eukaryotic Translation ◽  
Codon Recognition ◽  
Terminal Domain ◽  
Class 1 ◽  
Stop Codon Recognition ◽  
Stop Codon Reassignment

One factor involved in eukaryotic translation termination is class 1 release factor in eukaryotes (eRF1), which functions to decode stop codons. Variant code species, such as ciliates, frequently exhibit altered stop codon recognition. Studies revealed that some class-specific residues in the eRF1 N-terminal domain are responsible for stop codon reassignment in ciliates. Here, we investigated the effects on stop codon recognition of chimeric eRF1s containing the N-terminal domain of Euplotes octocarinatus and Blepharisma japonicum eRF1 fused to Saccharomyces cerevisiae M and C domains using dual luciferase read-through assays. Mutation of class-specific residues in different eRF1 classes was also studied to identify key residues and motifs involved in stop codon decoding. As expected, our results demonstrate that 3 pockets within the eRF1 N-terminal domain were involved in decoding stop codon nucleotides. However, allocation of residues to each pocket was revalued. Our data suggest that hydrophobic and class-specific surface residues participate in different functions: modulation of pocket conformation and interaction with stop codon nucleotides, respectively. Residues conserved across all eRF1s determine the relative orientation of the 3 pockets according to stop codon nucleotides. However, quantitative analysis of variant ciliate and yeast eRF1 point mutants did not reveal any correlation between evolutionary conservation of class-specific residues and termination-related functional specificity and was limited in elucidating a detailed mechanism for ciliate stop codon reassignment. Thus, based on isolation of suppressor tRNAs from Euplotes and Tetrahymena, we propose that stop codon reassignment in ciliates may be controlled by cooperation between eRF1 and suppressor tRNAs.

scholarly journals Thermodynamic and Kinetic Insights into Stop Codon Recognition by Release Factor 1

PLoS ONE ◽  
2014 ◽  
Vol 9 (4) ◽  
pp. e94058 ◽  
Author(s):  
Krista Trappl ◽  
Merrill A. Mathew ◽  
Simpson Joseph
Keyword(s):  
Stop Codon ◽  
Release Factor ◽  
Codon Recognition ◽  
Stop Codon Recognition

scholarly journals Nsp1 of SARS-CoV-2 Stimulates Host Translation Termination

2020 ◽  
Author(s):  
Alexey Shuvalov ◽  
Ekaterina Shuvalova ◽  
Nikita Biziaev ◽  
Elizaveta Sokolova ◽  
Konstantin Evmenov ◽  
...  
Keyword(s):  
Stop Codon ◽  
Translation Termination ◽  
Translation System ◽  
Release Factor ◽  
Viral Mrnas ◽  
Codon Recognition ◽  
Free Translation ◽  
Stop Codon Recognition ◽  
A Cell

ABSTRACTThe Nsp1 protein of SARS-CoV-2 regulates the translation of host and viral mRNAs in cells. Nsp1 inhibits host translation initiation by occluding the entry channel of the 40S ribosome subunit. The structural study of SARS-CoV-2 Nsp1-ribosomal complexes reported post-termination 80S complex containing Nsp1 and the eRF1 and ABCE1 proteins. Considering the presence of Nsp1 in the post-termination 80S ribosomal complex simultaneously with eRF1, we hypothesized that Nsp1 may be involved in translation termination. Using a cell-free translation system and reconstituted in vitro translation system, we show that Nsp1 stimulates translation termination in the stop codon recognition stage at all three stop codons. This stimulation targets the release factor 1 (eRF1) and does not affect the release factor 3 (eRF3). The activity of Nsp1 in translation termination is provided by its N-terminal domain and the minimal required part of eRF1 is NM domain. We assume that biological meaning of Nsp1 activity in translation termination is binding with the 80S ribosomes translating host mRNAs and removal them from the pool of the active ribosomes.

Structure-Based Energetics of Stop Codon Recognition by Eukaryotic Release Factor

2017 ◽  
Vol 57 (9) ◽  
pp. 2321-2328 ◽  
Author(s):  
Amit Kumar ◽  
Debadrita Basu ◽  
Priyadarshi Satpati
Keyword(s):  
Stop Codon ◽  
Release Factor ◽  
Codon Recognition ◽  
Stop Codon Recognition
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