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Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans
In most eukaryotic organisms, translation elongation requires two highly conserved elongation factors eEF1A and eEF2. Fungal systems are unique in requiring a third factor, the eukaryotic Elongation Factor 3 (eEF3). For decades, eEF3, a ribosome-dependent ATPase, was considered “fungal-specific”, ho...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5754060/ https://www.ncbi.nlm.nih.gov/pubmed/29300771 http://dx.doi.org/10.1371/journal.pone.0190524 |
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author | Mateyak, Maria K. Pupek, Justyna K. Garino, Alexandra E. Knapp, McCllelan C. Colmer, Sarah F. Kinzy, Terri Goss Dunaway, Stephen |
author_facet | Mateyak, Maria K. Pupek, Justyna K. Garino, Alexandra E. Knapp, McCllelan C. Colmer, Sarah F. Kinzy, Terri Goss Dunaway, Stephen |
author_sort | Mateyak, Maria K. |
collection | PubMed |
description | In most eukaryotic organisms, translation elongation requires two highly conserved elongation factors eEF1A and eEF2. Fungal systems are unique in requiring a third factor, the eukaryotic Elongation Factor 3 (eEF3). For decades, eEF3, a ribosome-dependent ATPase, was considered “fungal-specific”, however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes. In order to determine whether divergent eEF3-like proteins from other eukaryotic organisms can provide the essential functions of eEF3 in budding yeast, the eEF3-like proteins from Schizosaccharomyes pombe and an oomycete, Phytophthora infestans, were cloned and expressed in Saccharomyces cerevisiae. Plasmid shuffling experiments showed that both S. pombe and P. infestans eEF3 can support the growth of S. cerevisiae in the absence of endogenous budding yeast eEF3. Consistent with its ability to provide the essential functions of eEF3, P. infestans eEF3 possessed ribosome-dependent ATPase activity. Yeast cells expressing P. infestans eEF3 displayed reduced protein synthesis due to defects in translation elongation/termination. Identification of eEF3 in divergent species will advance understanding of its function and the ribosome specific determinants that lead to its requirement as well as contribute to the identification of functional domains of eEF3 for potential drug discovery. |
format | Online Article Text |
id | pubmed-5754060 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-57540602018-01-26 Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans Mateyak, Maria K. Pupek, Justyna K. Garino, Alexandra E. Knapp, McCllelan C. Colmer, Sarah F. Kinzy, Terri Goss Dunaway, Stephen PLoS One Research Article In most eukaryotic organisms, translation elongation requires two highly conserved elongation factors eEF1A and eEF2. Fungal systems are unique in requiring a third factor, the eukaryotic Elongation Factor 3 (eEF3). For decades, eEF3, a ribosome-dependent ATPase, was considered “fungal-specific”, however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes. In order to determine whether divergent eEF3-like proteins from other eukaryotic organisms can provide the essential functions of eEF3 in budding yeast, the eEF3-like proteins from Schizosaccharomyes pombe and an oomycete, Phytophthora infestans, were cloned and expressed in Saccharomyces cerevisiae. Plasmid shuffling experiments showed that both S. pombe and P. infestans eEF3 can support the growth of S. cerevisiae in the absence of endogenous budding yeast eEF3. Consistent with its ability to provide the essential functions of eEF3, P. infestans eEF3 possessed ribosome-dependent ATPase activity. Yeast cells expressing P. infestans eEF3 displayed reduced protein synthesis due to defects in translation elongation/termination. Identification of eEF3 in divergent species will advance understanding of its function and the ribosome specific determinants that lead to its requirement as well as contribute to the identification of functional domains of eEF3 for potential drug discovery. Public Library of Science 2018-01-04 /pmc/articles/PMC5754060/ /pubmed/29300771 http://dx.doi.org/10.1371/journal.pone.0190524 Text en © 2018 Mateyak et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Mateyak, Maria K. Pupek, Justyna K. Garino, Alexandra E. Knapp, McCllelan C. Colmer, Sarah F. Kinzy, Terri Goss Dunaway, Stephen Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans |
title | Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans |
title_full | Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans |
title_fullStr | Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans |
title_full_unstemmed | Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans |
title_short | Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans |
title_sort | demonstration of translation elongation factor 3 activity from a non-fungal species, phytophthora infestans |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5754060/ https://www.ncbi.nlm.nih.gov/pubmed/29300771 http://dx.doi.org/10.1371/journal.pone.0190524 |
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