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The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains

BACKGROUND: The genomes of the three parasitic protozoa Trypanosoma cruzi, Trypanosoma brucei and Leishmania major are the main subject of this study. These parasites are responsible for devastating human diseases known as Chagas disease, African sleeping sickness and cutaneous Leishmaniasis, respec...

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Autores principales: Brenchley, Rachel, Tariq, Humera, McElhinney, Helen, Szöőr, Balázs, Huxley-Jones, Julie, Stevens, Robert, Matthews, Keith, Tabernero, Lydia
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175518/
https://www.ncbi.nlm.nih.gov/pubmed/18039372
http://dx.doi.org/10.1186/1471-2164-8-434
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author Brenchley, Rachel
Tariq, Humera
McElhinney, Helen
Szöőr, Balázs
Huxley-Jones, Julie
Stevens, Robert
Matthews, Keith
Tabernero, Lydia
author_facet Brenchley, Rachel
Tariq, Humera
McElhinney, Helen
Szöőr, Balázs
Huxley-Jones, Julie
Stevens, Robert
Matthews, Keith
Tabernero, Lydia
author_sort Brenchley, Rachel
collection PubMed
description BACKGROUND: The genomes of the three parasitic protozoa Trypanosoma cruzi, Trypanosoma brucei and Leishmania major are the main subject of this study. These parasites are responsible for devastating human diseases known as Chagas disease, African sleeping sickness and cutaneous Leishmaniasis, respectively, that affect millions of people in the developing world. The prevalence of these neglected diseases results from a combination of poverty, inadequate prevention and difficult treatment. Protein phosphorylation is an important mechanism of controlling the development of these kinetoplastids. With the aim to further our knowledge of the biology of these organisms we present a characterisation of the phosphatase complement (phosphatome) of the three parasites. RESULTS: An ontology-based scan of the three genomes was used to identify 86 phosphatase catalytic domains in T. cruzi, 78 in T. brucei, and 88 in L. major. We found interesting differences with other eukaryotic genomes, such as the low proportion of tyrosine phosphatases and the expansion of the serine/threonine phosphatase family. Additionally, a large number of atypical protein phosphatases were identified in these species, representing more than one third of the total phosphatase complement. Most of the atypical phosphatases belong to the dual-specificity phosphatase (DSP) family and show considerable divergence from classic DSPs in both the domain organisation and sequence features. CONCLUSION: The analysis of the phosphatome of the three kinetoplastids indicates that they possess orthologues to many of the phosphatases reported in other eukaryotes, including humans. However, novel domain architectures and unusual combinations of accessory domains, suggest distinct functional roles for several of the kinetoplastid phosphatases, which await further experimental exploration. These distinct traits may be exploited in the selection of suitable new targets for drug development to prevent transmission and spread of the diseases, taking advantage of the already extensive knowledge on protein phosphatase inhibitors.
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spelling pubmed-21755182008-01-08 The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains Brenchley, Rachel Tariq, Humera McElhinney, Helen Szöőr, Balázs Huxley-Jones, Julie Stevens, Robert Matthews, Keith Tabernero, Lydia BMC Genomics Research Article BACKGROUND: The genomes of the three parasitic protozoa Trypanosoma cruzi, Trypanosoma brucei and Leishmania major are the main subject of this study. These parasites are responsible for devastating human diseases known as Chagas disease, African sleeping sickness and cutaneous Leishmaniasis, respectively, that affect millions of people in the developing world. The prevalence of these neglected diseases results from a combination of poverty, inadequate prevention and difficult treatment. Protein phosphorylation is an important mechanism of controlling the development of these kinetoplastids. With the aim to further our knowledge of the biology of these organisms we present a characterisation of the phosphatase complement (phosphatome) of the three parasites. RESULTS: An ontology-based scan of the three genomes was used to identify 86 phosphatase catalytic domains in T. cruzi, 78 in T. brucei, and 88 in L. major. We found interesting differences with other eukaryotic genomes, such as the low proportion of tyrosine phosphatases and the expansion of the serine/threonine phosphatase family. Additionally, a large number of atypical protein phosphatases were identified in these species, representing more than one third of the total phosphatase complement. Most of the atypical phosphatases belong to the dual-specificity phosphatase (DSP) family and show considerable divergence from classic DSPs in both the domain organisation and sequence features. CONCLUSION: The analysis of the phosphatome of the three kinetoplastids indicates that they possess orthologues to many of the phosphatases reported in other eukaryotes, including humans. However, novel domain architectures and unusual combinations of accessory domains, suggest distinct functional roles for several of the kinetoplastid phosphatases, which await further experimental exploration. These distinct traits may be exploited in the selection of suitable new targets for drug development to prevent transmission and spread of the diseases, taking advantage of the already extensive knowledge on protein phosphatase inhibitors. BioMed Central 2007-11-26 /pmc/articles/PMC2175518/ /pubmed/18039372 http://dx.doi.org/10.1186/1471-2164-8-434 Text en Copyright © 2007 Brenchley et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Brenchley, Rachel
Tariq, Humera
McElhinney, Helen
Szöőr, Balázs
Huxley-Jones, Julie
Stevens, Robert
Matthews, Keith
Tabernero, Lydia
The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains
title The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains
title_full The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains
title_fullStr The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains
title_full_unstemmed The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains
title_short The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains
title_sort tritryp phosphatome: analysis of the protein phosphatase catalytic domains
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2175518/
https://www.ncbi.nlm.nih.gov/pubmed/18039372
http://dx.doi.org/10.1186/1471-2164-8-434
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