The release of polypeptide chains from ribosomes in cell-free amino acid-incorporating systems by specific combinations of bases in synthetic polyribonucleotides.

Takanami, Mituru; Yan, Yonhon

doi:10.1073/pnas.54.5.1450

Cited by 26 publications

(5 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The fact that Met-tRNAM does form a com-plex with the elongation factors, whereas Met-tRNAF does not, indicates that the factors discriminate against tRNAF PEPTIDE CHAIN TERMINATION During chain elongation, the growing polypeptide chain remains linked to tRNA and bound to the mRNA-ribosome complex. After completion, the polypeptide is released from both of these bonds in the course of a composite process called peptide chain termination (116,191,203,376,425). Termination is apparently triggered when in the course of the movement of the ribosome along the mRNA a chain termination signal is reached at the A site of the 30S subunit (Fig.…”

Section: Translocationmentioning

confidence: 99%

Mechanism of protein biosynthesis.

Lengyel¹,

Söll²

1969

Bacteriological Reviews

133

View full text Add to dashboard Cite

Section: Translocationmentioning

confidence: 99%

Mechanism of protein biosynthesis.

Lengyel¹,

Söll²

1969

Bacteriological Reviews

133

View full text Add to dashboard Cite

“…Then all three nonsense codons: UAA, UAG (Weigert and Garen, 1965) and UGA (Brenner et al, 1967) were identified. The presence of these triplets in mRNA were shown to serve in vitro as signals for release of polypeptide chains from ribosomes (Takanami and Yan, 1965) and did not code for any aminoacids (Khorana, 1968). Nonsense triplets were shown to be recognized by specific proteins called release factors (Capecchi, 1967), two of which had different codon specificities: RF1 (UAA, UAG) and RF2 (UAA, UGA) (Scolnick et al, 1968).…”

Section: Concepts and Facts Came First From Prokaryotesmentioning

confidence: 99%

Eukaryotic release factors (eRFs) history

Инге-Вечтомов

Zhouravleva

Maury

2003

Biology of the Cell

114

View full text Add to dashboard Cite

In the present review, we describe the history of the identification of the eukaryotic translation termination factors eRF1 and eRF3. As in the case of several proteins involved in general and essential processes in all cells (e.g., DNA replication, gene expression regulation...) the strategies and methodologies used to identify these release factors were first established in prokaryotes. The genetic investigations in Saccharomyces cerevisiae have made a major contribution in the field. A large amount of data have been produced, from which it was concluded that the SUP45 and SUP35 genes were controlling translation termination but were also involved in other functions important for the cell organization and the cell cycle accomplishment. This does not seem to be restricted to yeast but is also probably the case in eukaryotes in general. The biochemical studies of the proteins encoded by the higher eukaryote homologs of SUP45 and SUP35 were efficient and permitted the identification of eRF1 as being the key protein in the termination process, eRF3 having a stimulating role. Around 25 years were needed after the identification of sup45 and sup35 mutants for the characterization of their gene products as eRF1 and eRF3, respectively. It also has to be pointed out that if the results came first from bacteria, the identification of RF3 and eRF3 was made practically at the same time. Moreover, eRF1 was the first crystal structure obtained for a class-1 release factor, the bacterial RF2 structure came later. The goal is now to understand at the molecular level the roles of both eRF1 and eRF3 in addition to their translation termination functions.

show abstract

“…Three triplets-UAA, UAG (Weigert and Garen 1965), and UGA (Brenner et al 1967)-were identified as nonsense stop codons and shown to serve in vitro as signals for the release of polypeptide from the ribosome (Takanami and Yan 1965). The misincorporation of an amino acid at the stop codon occurs at a frequency of $10 À4 and is called readthrough.…”

mentioning

confidence: 99%

Fine-Tuning of Translation Termination Efficiency inSaccharomyces cerevisiaeInvolves Two Factors in Close Proximity to the Exit Tunnel of the Ribosome

et al. 2007

View full text Add to dashboard Cite

In eukaryotes, release factors 1 and 3 (eRF1 and eRF3) are recruited to promote translation termination when a stop codon on the mRNA enters at the ribosomal A-site. However, their overexpression increases termination efficiency only moderately, suggesting that other factors might be involved in the termination process. To determine such unknown components, we performed a genetic screen in Saccharomyces cerevisiae that identified genes increasing termination efficiency when overexpressed. For this purpose, we constructed a dedicated reporter strain in which a leaky stop codon is inserted into the chromosomal copy of the ade2 gene. Twenty-five antisuppressor candidates were identified and characterized for their impact on readthrough. Among them, SSB1 and snR18, two factors close to the exit tunnel of the ribosome, directed the strongest antisuppression effects when overexpressed, showing that they may be involved in fine-tuning of the translation termination level.

show abstract

The release of polypeptide chains from ribosomes in cell-free amino acid-incorporating systems by specific combinations of bases in synthetic polyribonucleotides.

Cited by 26 publications

References 12 publications

Mechanism of protein biosynthesis.

Mechanism of protein biosynthesis.

Eukaryotic release factors (eRFs) history

Fine-Tuning of Translation Termination Efficiency inSaccharomyces cerevisiaeInvolves Two Factors in Close Proximity to the Exit Tunnel of the Ribosome

Contact Info

Product

Resources

About