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A Comprehensive Phylogenetic Analysis of Deadenylases

Deadenylases catalyze the shortening of the poly(A) tail at the messenger ribonucleic acid (mRNA) 3′-end in eukaryotes. Therefore, these enzymes influence mRNA decay, and constitute a major emerging group of promising anti-cancer pharmacological targets. Herein, we conducted full phylogenetic analys...

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Autores principales: Pavlopoulou, Athanasia, Vlachakis, Dimitrios, Balatsos, Nikolaos A.A., Kossida, Sophia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Libertas Academica 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3859875/
https://www.ncbi.nlm.nih.gov/pubmed/24348009
http://dx.doi.org/10.4137/EBO.S12746
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author Pavlopoulou, Athanasia
Vlachakis, Dimitrios
Balatsos, Nikolaos A.A.
Kossida, Sophia
author_facet Pavlopoulou, Athanasia
Vlachakis, Dimitrios
Balatsos, Nikolaos A.A.
Kossida, Sophia
author_sort Pavlopoulou, Athanasia
collection PubMed
description Deadenylases catalyze the shortening of the poly(A) tail at the messenger ribonucleic acid (mRNA) 3′-end in eukaryotes. Therefore, these enzymes influence mRNA decay, and constitute a major emerging group of promising anti-cancer pharmacological targets. Herein, we conducted full phylogenetic analyses of the deadenylase homologs in all available genomes in an effort to investigate evolutionary relationships between the deadenylase families and to identify invariant residues, which probably play key roles in the function of deadenylation across species. Our study includes both major Asp-Glu-Asp-Asp (DEDD) and exonuclease-endonuclease-phospatase (EEP) deadenylase superfamilies. The phylogenetic analysis has provided us with important information regarding conserved and invariant deadenylase amino acids across species. Knowledge of the phylogenetic properties and evolution of the domain of deadenylases provides the foundation for the targeted drug design in the pharmaceutical industry and modern exonuclease anti-cancer scientific research.
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spelling pubmed-38598752013-12-12 A Comprehensive Phylogenetic Analysis of Deadenylases Pavlopoulou, Athanasia Vlachakis, Dimitrios Balatsos, Nikolaos A.A. Kossida, Sophia Evol Bioinform Online Original Research Deadenylases catalyze the shortening of the poly(A) tail at the messenger ribonucleic acid (mRNA) 3′-end in eukaryotes. Therefore, these enzymes influence mRNA decay, and constitute a major emerging group of promising anti-cancer pharmacological targets. Herein, we conducted full phylogenetic analyses of the deadenylase homologs in all available genomes in an effort to investigate evolutionary relationships between the deadenylase families and to identify invariant residues, which probably play key roles in the function of deadenylation across species. Our study includes both major Asp-Glu-Asp-Asp (DEDD) and exonuclease-endonuclease-phospatase (EEP) deadenylase superfamilies. The phylogenetic analysis has provided us with important information regarding conserved and invariant deadenylase amino acids across species. Knowledge of the phylogenetic properties and evolution of the domain of deadenylases provides the foundation for the targeted drug design in the pharmaceutical industry and modern exonuclease anti-cancer scientific research. Libertas Academica 2013-12-02 /pmc/articles/PMC3859875/ /pubmed/24348009 http://dx.doi.org/10.4137/EBO.S12746 Text en © 2013 the author(s), publisher and licensee Libertas Academica Ltd. This is an open access article published under the Creative Commons CC-BY-NC 3.0 license.
spellingShingle Original Research
Pavlopoulou, Athanasia
Vlachakis, Dimitrios
Balatsos, Nikolaos A.A.
Kossida, Sophia
A Comprehensive Phylogenetic Analysis of Deadenylases
title A Comprehensive Phylogenetic Analysis of Deadenylases
title_full A Comprehensive Phylogenetic Analysis of Deadenylases
title_fullStr A Comprehensive Phylogenetic Analysis of Deadenylases
title_full_unstemmed A Comprehensive Phylogenetic Analysis of Deadenylases
title_short A Comprehensive Phylogenetic Analysis of Deadenylases
title_sort comprehensive phylogenetic analysis of deadenylases
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3859875/
https://www.ncbi.nlm.nih.gov/pubmed/24348009
http://dx.doi.org/10.4137/EBO.S12746
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