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Functional Role of UPF2 Phosphorylated Regions in Translation Termination in Yeast
Author(s) -
Haddock Luis Antonio,
ColónMorales Edgardo M,
Lasalde Clarivel,
Lin Qishan,
González Carlos I
Publication year - 2016
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.30.1_supplement.1055.4
Subject(s) - biology , nonsense mediated decay , translation (biology) , saccharomyces cerevisiae , frameshift mutation , microbiology and biotechnology , phosphorylation , genetics , messenger rna , mutation , rna splicing , yeast , gene , rna
Eukaryotes have evolved a unique mechanism for recognizing premature termination codons (PTC) present in the mRNA. These PTC‐containing mRNAs are recognized and degraded by a mechanism known as nonsense‐mediated mRNA decay (NMD), which prevents the formation and accumulation of non‐functional or truncated proteins that can be the starting point for several human diseases, such as Cystic Fibrosis and Duchenne Muscular Dystrophy. One of the proteins involved in NMD is the up‐frameshift protein 2 ( UPF2 ), which has been shown to be phosphorylated and essential for the accuracy of translation termination. However, the functional role of Upf2 phosphorylated residues in the translational termination accuracy is still unknown. To test this, we generated deletions of several UPF2 regions containing phosphorylated residues and measured the growth rate of a Saccharomyces cerevisiae strain that harbors the can1‐100 allele in the presence of canavanine. Results demonstrated that deletion of the regions in Upf2 corresponding to amino acids (aa) 50–59 and 421–430, showed less growth due to a higher sensitivity to canavanine caused by a faulty translation termination. This suggests that these Upf2 regions are crucial for translation termination accuracy and provide a foundation for future studies to determine the role of Upf2 phosphorylation in the fidelity of translation termination in eukaryotes.