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Genome wide in silico analysis of Plasmodium falciparum phosphatome
BACKGROUND: Eukaryotic cellular machineries are intricately regulated by several molecular mechanisms involving transcriptional control, post-translational control and post-translational modifications of proteins (PTMs). Reversible protein phosphorylation/dephosphorylation process, which involves ki...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4256932/ https://www.ncbi.nlm.nih.gov/pubmed/25425018 http://dx.doi.org/10.1186/1471-2164-15-1024 |
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author | Pandey, Rajan Mohmmed, Asif Pierrot, Christine Khalife, Jamal Malhotra, Pawan Gupta, Dinesh |
author_facet | Pandey, Rajan Mohmmed, Asif Pierrot, Christine Khalife, Jamal Malhotra, Pawan Gupta, Dinesh |
author_sort | Pandey, Rajan |
collection | PubMed |
description | BACKGROUND: Eukaryotic cellular machineries are intricately regulated by several molecular mechanisms involving transcriptional control, post-translational control and post-translational modifications of proteins (PTMs). Reversible protein phosphorylation/dephosphorylation process, which involves kinases as well as phosphatases, represents an important regulatory mechanism for diverse pathways and systems in all organisms including human malaria parasite, Plasmodium falciparum. Earlier analysis on P. falciparum protein-phosphatome revealed presence of 34 phosphatases in Plasmodium genome. Recently, we re-analysed P. falciparum phosphatome aimed at identifying parasite specific phosphatases. RESULTS: Plasmodium database (PlasmoDB 9.2) search, combined with PFAM and CDD searches, revealed 67 candidate phosphatases in P. falciparum. While this number is far less than the number of phosphatases present in Homo sapiens, it is almost the same as in other Plasmodium species. These Plasmodium phosphatase proteins were classified into 13 super families based on NCBI CDD search. Analysis of proteins expression profiles of the 67 phosphatases revealed that 44 phosphatases are expressed in both schizont as well as gametocytes stages. Fourteen phosphatases are common in schizont, ring and trophozoite stages, four phosphatases are restricted to gametocytes, whereas another three restricted to schizont stage. The phylogenetic trees for each of the known phosphatase super families reveal a considerable phylogenetic closeness amongst apicomplexan organisms and a considerable phylogenetic distance with other eukaryotic model organisms included in the study. The GO assignments and predicted interaction partners of the parasite phosphatases indicate its important role in diverse cellular processes. CONCLUSION: In the study presented here, we reviewed the P. falciparum phosphatome to show presence of 67 candidate phosphatases in P. falciparum genomes/proteomes. Intriguingly, amongst these phosphatases, we could identify six Plasmodium specific phosphatases and 33 putative phosphatases that do not have human orthologs, thereby suggesting that these phosphatases have the potential to be explored as novel antimalarial drug targets. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/1471-2164-15-1024) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4256932 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-42569322014-12-06 Genome wide in silico analysis of Plasmodium falciparum phosphatome Pandey, Rajan Mohmmed, Asif Pierrot, Christine Khalife, Jamal Malhotra, Pawan Gupta, Dinesh BMC Genomics Research Article BACKGROUND: Eukaryotic cellular machineries are intricately regulated by several molecular mechanisms involving transcriptional control, post-translational control and post-translational modifications of proteins (PTMs). Reversible protein phosphorylation/dephosphorylation process, which involves kinases as well as phosphatases, represents an important regulatory mechanism for diverse pathways and systems in all organisms including human malaria parasite, Plasmodium falciparum. Earlier analysis on P. falciparum protein-phosphatome revealed presence of 34 phosphatases in Plasmodium genome. Recently, we re-analysed P. falciparum phosphatome aimed at identifying parasite specific phosphatases. RESULTS: Plasmodium database (PlasmoDB 9.2) search, combined with PFAM and CDD searches, revealed 67 candidate phosphatases in P. falciparum. While this number is far less than the number of phosphatases present in Homo sapiens, it is almost the same as in other Plasmodium species. These Plasmodium phosphatase proteins were classified into 13 super families based on NCBI CDD search. Analysis of proteins expression profiles of the 67 phosphatases revealed that 44 phosphatases are expressed in both schizont as well as gametocytes stages. Fourteen phosphatases are common in schizont, ring and trophozoite stages, four phosphatases are restricted to gametocytes, whereas another three restricted to schizont stage. The phylogenetic trees for each of the known phosphatase super families reveal a considerable phylogenetic closeness amongst apicomplexan organisms and a considerable phylogenetic distance with other eukaryotic model organisms included in the study. The GO assignments and predicted interaction partners of the parasite phosphatases indicate its important role in diverse cellular processes. CONCLUSION: In the study presented here, we reviewed the P. falciparum phosphatome to show presence of 67 candidate phosphatases in P. falciparum genomes/proteomes. Intriguingly, amongst these phosphatases, we could identify six Plasmodium specific phosphatases and 33 putative phosphatases that do not have human orthologs, thereby suggesting that these phosphatases have the potential to be explored as novel antimalarial drug targets. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/1471-2164-15-1024) contains supplementary material, which is available to authorized users. BioMed Central 2014-11-25 /pmc/articles/PMC4256932/ /pubmed/25425018 http://dx.doi.org/10.1186/1471-2164-15-1024 Text en © Pandey et al.; licensee BioMed Central Ltd. 2014 This article is published under license to BioMed Central Ltd. 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 work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Pandey, Rajan Mohmmed, Asif Pierrot, Christine Khalife, Jamal Malhotra, Pawan Gupta, Dinesh Genome wide in silico analysis of Plasmodium falciparum phosphatome |
title | Genome wide in silico analysis of Plasmodium falciparum phosphatome |
title_full | Genome wide in silico analysis of Plasmodium falciparum phosphatome |
title_fullStr | Genome wide in silico analysis of Plasmodium falciparum phosphatome |
title_full_unstemmed | Genome wide in silico analysis of Plasmodium falciparum phosphatome |
title_short | Genome wide in silico analysis of Plasmodium falciparum phosphatome |
title_sort | genome wide in silico analysis of plasmodium falciparum phosphatome |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4256932/ https://www.ncbi.nlm.nih.gov/pubmed/25425018 http://dx.doi.org/10.1186/1471-2164-15-1024 |
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