Studies on human eRF3-PABP interaction reveal the influence of eRF3a N-terminal glycin repeat on eRF3-PABP binding affinity and the lower affinity of eRF3a 12-GGC allele involved in cancer susceptibility

Jerbi, Soumaya; Jollès, Béatrice; Bouceba, Tahar; Jean-Jean, Olivier

doi:10.1080/15476286.2015.1137421

Cited by 12 publications

(10 citation statements)

References 36 publications

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“…A role for Pab1 in restricting readthrough is consistent with several earlier studies in multiple systems, including those reporting: a) position dependence of the noncanonical genetic codes in Ciliates (alluded to above) (Heaphy et al, 2016;Swart et al, 2016;Zahonova et al, 2016), b) interactions between eRF3 and PABP from mammalian, Xenopus, and yeast cells, and identification of specific interacting domains in the respective proteins, using two-hybrid, co-immunoprecipitation, isothermal titration calorimetry, and surface plasmon resonance methodologies (Cosson et al, 2002a;Cosson et al, 2002b;Hoshino et al, 1999;Hosoda et al, 2003;Jerbi et al, 2016;Kononenko et al, 2010;Roque et al, 2015;Uchida et al, 2002), and c) direct stimulation of peptidyl-tRNA hydrolysis dependent on eRF3:PABP interaction in a reconstituted cellfree system (Ivanov et al, 2016). However, our results differ from those of Roque et al who found that readthrough efficiency in a dual luciferase assay in yeast decreased when Pab1:eRF3 interaction was interrupted (Roque et al, 2015).…”

Section: Yeast Pab1 Is a Key Determinant Of The Ptc Position Effectsupporting

confidence: 86%

Nonsense suppression position effect implicates poly(A)-binding protein in the regulation of translation termination

Roy

et al. 2019

Preprint

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Readthrough of translation termination codons, also known as nonsense suppression, is a relatively inefficient process mediated by ribosomal A site recognition and insertion of near-cognate tRNAs. Multiple factors influence readthrough efficiency, including nonsense codon specificity and context. To determine whether nonsense codon position in a gene influences the extent of readthrough, we generated a series of LUC nonsense alleles and quantitated both readthrough and termination efficiencies at each nonsense codon in yeast cells lacking nonsense-mediated mRNA decay (NMD) activity.Readthrough efficiency for premature termination codons (PTCs) manifested a marked dependence on PTC proximity to the mRNA 3'-end, decreasing progressively across the LUC ORF but increasing with 3'-UTR lengthening. These effects were eliminated, and translation termination efficiency decreased considerably, in cells harboring pab1 mutations. Our results support a critical role for poly(A)-binding protein in the regulation of translation termination and suggest that inefficient termination is the trigger for NMD.3

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Section: Yeast Pab1 Is a Key Determinant Of The Ptc Position Effectsupporting

confidence: 86%

Nonsense suppression position effect implicates poly(A)-binding protein in the regulation of translation termination

Roy

et al. 2019

Preprint

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“…Obviously, the ribosome, upon reaching the stop codon, naturally occurs nearby PABP that is bound to the poly(A) tail. In turn, the PABP has a site for binding with eukaryotic release factor eRF3 , a GTPase, which interacts with the eRF1 and induces conformational rearrangement in the termination complex followed by peptide release . Furthermore, we have recently shown that PABP, via association with eRF3, dramatically improves the efficiency of eRF3 binding with the ribosome, which increases the total activity of the termination complex .…”

Section: Pabp and Short 3′utrs Ensure Termination In The Species Withmentioning

confidence: 99%

Reassigning stop codons via translation termination: How a few eukaryotes broke the dogma

Alkalaeva

Mikhailova

2016

BioEssays

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The genetic code determines how amino acids are encoded within mRNA. It is universal among the vast majority of organisms, although several exceptions are known. Variant genetic codes are found in ciliates, mitochondria, and numerous other organisms. All revealed genetic codes (standard and variant) have at least one codon encoding a translation stop signal. However, recently two new genetic codes with a reassignment of all three stop codons were revealed in studies examining the protozoa transcriptomes. Here, we discuss this finding and the recent studies of variant genetic codes in eukaryotes. We consider the possible molecular mechanisms allowing the use of certain codons as sense and stop signals simultaneously. The results obtained by studying these amazing organisms represent a new and exciting insight into the mechanism of stop codon decoding in eukaryotes. Also see the video abstract here.

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“…These findings have particular relevance to human disease, as it has been shown that allelic variants of eRF3a are associated with increased risk of certain cancers (Brito et al, ; Malta‐Vacas et al, ; Miri, Hemati, Safari, & Tavassoli, ). Furthermore, recombinant eRF3a containing such alleles has been shown to bind differentially to PABP, with one particular allelic variant exhibiting an eight‐fold lower binding affinity (Jerbi, Jolles, Bouceba, & Jean‐Jean, ), however, a relevant pathogenic mechanism has not yet been described.…”

Section: Rna Binding Proteins and Their Role In Translationmentioning

confidence: 99%

Trans‐acting translational regulatory RNA binding proteins

et al. 2018

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The canonical molecular machinery required for global mRNA translation and its control has been well defined, with distinct sets of proteins involved in the processes of translation initiation, elongation and termination. Additionally, noncanonical, trans‐acting regulatory RNA‐binding proteins (RBPs) are necessary to provide mRNA‐specific translation, and these interact with 5′ and 3′ untranslated regions and coding regions of mRNA to regulate ribosome recruitment and transit. Recently it has also been demonstrated that trans‐acting ribosomal proteins direct the translation of specific mRNAs. Importantly, it has been shown that subsets of RBPs often work in concert, forming distinct regulatory complexes upon different cellular perturbation, creating an RBP combinatorial code, which through the translation of specific subsets of mRNAs, dictate cell fate. With the development of new methodologies, a plethora of novel RNA binding proteins have recently been identified, although the function of many of these proteins within mRNA translation is unknown. In this review we will discuss these methodologies and their shortcomings when applied to the study of translation, which need to be addressed to enable a better understanding of trans‐acting translational regulatory proteins. Moreover, we discuss the protein domains that are responsible for RNA binding as well as the RNA motifs to which they bind, and the role of trans‐acting ribosomal proteins in directing the translation of specific mRNAs.This article is categorized under: RNA Interactions with Proteins and Other Molecules > RNA–Protein ComplexesTranslation > Translation RegulationTranslation > Translation Mechanisms

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Studies on human eRF3-PABP interaction reveal the influence of eRF3a N-terminal glycin repeat on eRF3-PABP binding affinity and the lower affinity of eRF3a 12-GGC allele involved in cancer susceptibility

Cited by 12 publications

References 36 publications

Nonsense suppression position effect implicates poly(A)-binding protein in the regulation of translation termination

Nonsense suppression position effect implicates poly(A)-binding protein in the regulation of translation termination

Reassigning stop codons via translation termination: How a few eukaryotes broke the dogma

Trans‐acting translational regulatory RNA binding proteins

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