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Deep Insight into the Phosphatomes of Parasitic Protozoa and a Web Resource ProtozPhosDB

Phosphorylation dynamically regulates the function of proteins by maintaining a balance between protein kinase and phosphatase activity. A comprehensive understanding of the role phosphatases in cellular signaling is lacking in case of protozoans of medical and veterinary importance worldwide. The d...

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Autores principales: Anwar, Tamanna, Gourinath, Samudrala
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5145157/
https://www.ncbi.nlm.nih.gov/pubmed/27930683
http://dx.doi.org/10.1371/journal.pone.0167594
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author Anwar, Tamanna
Gourinath, Samudrala
author_facet Anwar, Tamanna
Gourinath, Samudrala
author_sort Anwar, Tamanna
collection PubMed
description Phosphorylation dynamically regulates the function of proteins by maintaining a balance between protein kinase and phosphatase activity. A comprehensive understanding of the role phosphatases in cellular signaling is lacking in case of protozoans of medical and veterinary importance worldwide. The drugs used to treat protozoal diseases have many undesired effects and the development of resistance, highlights the need for new effective and safer antiprotozoal agents. In the present study we have analyzed phosphatomes of 15 protozoans of medical significance. We identified ~2000 phosphatases, out of which 21% are uncharacterized proteins. A significant positive correlation between phosphatome and proteome size was observed except for E. histolytica, having highest density of phosphatases irrespective of its proteome size. A difference in the number of phosphatases among different genera shows the variation in the signaling pathways they are involved in. The phosphatome of parasites is dominated by ser/thr phosphatases contrary to the vertebrate host dominated by tyrosine phosphatases. Phosphatases were widely distributed throughout the cell suggesting physiological adaptation of the parasite to regulate its host. 20% to 45% phosphatome of different protozoa consists of ectophosphatases, i.e. crucial for the survival of parasites. A database and a webserver “ProtozPhosDB” can be used to explore the phosphatomes of protozoans of medical significance.
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spelling pubmed-51451572016-12-22 Deep Insight into the Phosphatomes of Parasitic Protozoa and a Web Resource ProtozPhosDB Anwar, Tamanna Gourinath, Samudrala PLoS One Research Article Phosphorylation dynamically regulates the function of proteins by maintaining a balance between protein kinase and phosphatase activity. A comprehensive understanding of the role phosphatases in cellular signaling is lacking in case of protozoans of medical and veterinary importance worldwide. The drugs used to treat protozoal diseases have many undesired effects and the development of resistance, highlights the need for new effective and safer antiprotozoal agents. In the present study we have analyzed phosphatomes of 15 protozoans of medical significance. We identified ~2000 phosphatases, out of which 21% are uncharacterized proteins. A significant positive correlation between phosphatome and proteome size was observed except for E. histolytica, having highest density of phosphatases irrespective of its proteome size. A difference in the number of phosphatases among different genera shows the variation in the signaling pathways they are involved in. The phosphatome of parasites is dominated by ser/thr phosphatases contrary to the vertebrate host dominated by tyrosine phosphatases. Phosphatases were widely distributed throughout the cell suggesting physiological adaptation of the parasite to regulate its host. 20% to 45% phosphatome of different protozoa consists of ectophosphatases, i.e. crucial for the survival of parasites. A database and a webserver “ProtozPhosDB” can be used to explore the phosphatomes of protozoans of medical significance. Public Library of Science 2016-12-08 /pmc/articles/PMC5145157/ /pubmed/27930683 http://dx.doi.org/10.1371/journal.pone.0167594 Text en © 2016 Anwar, Gourinath 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
Anwar, Tamanna
Gourinath, Samudrala
Deep Insight into the Phosphatomes of Parasitic Protozoa and a Web Resource ProtozPhosDB
title Deep Insight into the Phosphatomes of Parasitic Protozoa and a Web Resource ProtozPhosDB
title_full Deep Insight into the Phosphatomes of Parasitic Protozoa and a Web Resource ProtozPhosDB
title_fullStr Deep Insight into the Phosphatomes of Parasitic Protozoa and a Web Resource ProtozPhosDB
title_full_unstemmed Deep Insight into the Phosphatomes of Parasitic Protozoa and a Web Resource ProtozPhosDB
title_short Deep Insight into the Phosphatomes of Parasitic Protozoa and a Web Resource ProtozPhosDB
title_sort deep insight into the phosphatomes of parasitic protozoa and a web resource protozphosdb
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5145157/
https://www.ncbi.nlm.nih.gov/pubmed/27930683
http://dx.doi.org/10.1371/journal.pone.0167594
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