The translational stop signal: Codon with a context, or extended factor recognition element?

Tate, Warren P.; Poole, Elizabeth S.; Dalphin, Mark E.; Major, Louise L.; Crawford, Damion; Mannering, Sally A.

doi:10.1016/s0300-9084(97)86716-8

Cited by 60 publications

(53 citation statements)

References 27 publications

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“…Numerous studies indicated that the nucleotide immediately following the stop codon (defined as +4) was a crucial determinant of termination efficiency Bonetti et al, 1995;Tate et al, 1996). Prokaryotes have a preference to U in the base following the stop codons (Brown et al, 1990).…”

Section: The Biased Bases Around the Stop Codonsmentioning

confidence: 99%

Comparative analysis of base biases around the stop codons in six eukaryotes

Liu

2005

Biosystems

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Section: The Biased Bases Around the Stop Codonsmentioning

confidence: 99%

Comparative analysis of base biases around the stop codons in six eukaryotes

Liu

2005

Biosystems

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“…Moreover, it has been shown that the context of the stop codon played an important role in the efficiency of the termination reaction (reviewed in Refs. [44][45][46]). This was perhaps first evident from the markedly differing levels of stop codon readthrough by suppressor tRNAs depending on the context of the stop codon, both upstream and downstream.…”

Section: Codon Recognition Domain Of Bacterial Rfs: the Termination Smentioning

confidence: 99%

Termination and Ribosome Recycling

Wilson

2004

Protein Synthesis and Ribosome Structure

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“…An in-frame UGA codon inside the prfB gene allows many eubacteria to autoregulate exquisitely the synthesis of their own release factors by a ϩ 1 frameshift in the recoding site (Craigen and Caskey, 1986). Only recently, the crystal structures of the human eukaryotic release factor eRF1 and the bacterial RF2 confirmed the proposed tRNA-protein mimicry hypothesis, in which release factor anticodon determinants play a crucial role in stop codon recognition (Moffat and Tate 1994;Ito et al, 1996;Tate et al, 1996;Song et al, 2000;Vestergaard et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

A Peptide Chain Release Factor 2 Affects the Stability of UGA-Containing Transcripts in Arabidopsis Chloroplasts

et al. 2002

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Positional cloning of the hcf109 ( high chlorophyll fluorescence ) mutation in Arabidopsis has identified a nucleus-encoded, plastid-localized release factor 2-like protein, AtprfB, indicating that the processes of translational termination in chloroplasts resemble those of eubacteria. Control of atprfB expression by light and tissues is connected to chloroplast development. A point mutation at the last nucleotide of the second intron causes a new splice site farther downstream, resulting in a deletion of seven amino acid residues in the N-terminal region of the Hcf109 protein. The mutation causes decreased stability of UGA-containing mRNAs. Our data suggest that transcripts with UGA stop codons are terminated exclusively by AtprfB in chloroplasts and that AtprfB is involved in the regulation of both mRNA stability and protein synthesis. Furthermore, sequence data reveal a ؉ 1 frameshift at an internal in-frame TGA stop codon in the progenitor prfB gene of cyanobacteria. The expression pattern and functions of atprfB could reflect evolutionary driving forces toward the conservation of TGA stop codons exclusively in plastid genomes of land plants.

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The translational stop signal: Codon with a context, or extended factor recognition element?

Cited by 60 publications

References 27 publications

Comparative analysis of base biases around the stop codons in six eukaryotes

Comparative analysis of base biases around the stop codons in six eukaryotes

Termination and Ribosome Recycling

A Peptide Chain Release Factor 2 Affects the Stability of UGA-Containing Transcripts in Arabidopsis Chloroplasts

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