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

RNA Biology
Soumaya JerbiOlivier Jean-Jean

Abstract

The eukaryotic release factor 3 (eRF3) has been involved in the control of mRNA degradation through its association with the cytoplasmic Poly(A) Binding Protein, PABP. In mammals, eRF3 N-terminal domain contains two overlapping PAM2 motifs which specifically recognize the MLLE domain of PABP. In humans, eRF3a/GSPT1 gene contains a stable GGC repeat encoding a repeat of glycine residues in eRF3a N-terminus. There are five known eRF3a/GSPT1 alleles in the human population, encoding 7, 9, 10, 11 and 12 glycines. Several studies have reported that the presence of eRF3a 12-GGC allele is correlated with an increased risk of cancer development. Using surface plasmon resonance, we have studied the interaction of the various allelic forms of eRF3a with PABP alone or poly(A)-bound PABP. We found that the N-terminal glycine repeat of eRF3a influences eRF3a-PABP interaction and that eRF3a 12-GGC allele has a decreased binding affinity for PABP. Our comparative analysis on eRF3a alleles suggests that the presence of eRF3a 12-GGC allele could modify the coupling between translation termination and mRNA deadenylation.

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Citations

Dec 24, 2016·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Elena Alkalaeva, Tatiana Mikhailova
Mar 3, 2018·International Journal of Molecular Sciences·Lucie CoppinPascal Pigny
Jan 18, 2018·Wiley Interdisciplinary Reviews. RNA·Robert F HarveyAnne E Willis
Feb 2, 2021·RNA Biology·Sandy MattijssenRichard J Maraia

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Methods Mentioned

BETA
GTPase
surface plasmon resonance
biosensor
chip
Exome Sequencing
affinity purification
PCR
chips
electrophoresis
X-ray

Software Mentioned

BIAevaluation
BIAevalution

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