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Identification of R2TP complex of Leishmania donovaniand Plasmodium falciparum using genome wide in-silico analysis
Recently discovered R2TP complex is an important multiprotein complex involved in multiple cellular process like snoRNP biogenesis, PIKK signaling, RNA polymerase II assembly and apoptosis. Within R2TP complex, Pih1 tightly interacts with Rvb1/Rvb2 and with Tah1 to form R2TP macromolecular complex....
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3913666/ https://www.ncbi.nlm.nih.gov/pubmed/24505500 http://dx.doi.org/10.4161/cib.26005 |
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author | Ahmad, Moaz Afrin, Farhat Tuteja, Renu |
author_facet | Ahmad, Moaz Afrin, Farhat Tuteja, Renu |
author_sort | Ahmad, Moaz |
collection | PubMed |
description | Recently discovered R2TP complex is an important multiprotein complex involved in multiple cellular process like snoRNP biogenesis, PIKK signaling, RNA polymerase II assembly and apoptosis. Within R2TP complex, Pih1 tightly interacts with Rvb1/Rvb2 and with Tah1 to form R2TP macromolecular complex. R2TP complex further interacts with Hsp90 to form R2TP-Hsp90 complex, which has been found critical in many cellular process. The genome wide screening of Leishmania donovani and Plasmodium falciparum led to the identification of RuvB like1, RuvB like 2, Pih1, and Tah1. Therefore, we speculate that this complex is also important for these parasites as in the yeast. The detailed analysis of crucial components of R2TP complex, Ld-RuvB like 1, and Ld-RuvB like 2, revealed the presence of characteristic motifs like DNA binding motif and ATPase motifs. Hsp90 is also reported from Leishmania donovani and Plasmodium falciparum suggesting that the R2TP complex further interacts with Hsp90 to form R2TP-Hsp90 complex. Recently it has been discovered that RuvB like proteins are overexpressed in many cancers and their ATPase activity is crucial for cancer cell proliferation and the human RuvBs have been proposed as suitable drug target for cancer. Similarly one of the Plasmodium falciparum RuvB like protein (PfRuvB3) has been found to be specific to the stage where nuclear division led multiplication of parasite take place. Considering all these it seems that the R2TP complex may be playing some critical role both in the cancer cell proliferation in human and rapid multiplication of the parasites Leishmania donovani and Plasmodium falciparum. |
format | Online Article Text |
id | pubmed-3913666 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-39136662014-02-06 Identification of R2TP complex of Leishmania donovaniand Plasmodium falciparum using genome wide in-silico analysis Ahmad, Moaz Afrin, Farhat Tuteja, Renu Commun Integr Biol Research Paper Recently discovered R2TP complex is an important multiprotein complex involved in multiple cellular process like snoRNP biogenesis, PIKK signaling, RNA polymerase II assembly and apoptosis. Within R2TP complex, Pih1 tightly interacts with Rvb1/Rvb2 and with Tah1 to form R2TP macromolecular complex. R2TP complex further interacts with Hsp90 to form R2TP-Hsp90 complex, which has been found critical in many cellular process. The genome wide screening of Leishmania donovani and Plasmodium falciparum led to the identification of RuvB like1, RuvB like 2, Pih1, and Tah1. Therefore, we speculate that this complex is also important for these parasites as in the yeast. The detailed analysis of crucial components of R2TP complex, Ld-RuvB like 1, and Ld-RuvB like 2, revealed the presence of characteristic motifs like DNA binding motif and ATPase motifs. Hsp90 is also reported from Leishmania donovani and Plasmodium falciparum suggesting that the R2TP complex further interacts with Hsp90 to form R2TP-Hsp90 complex. Recently it has been discovered that RuvB like proteins are overexpressed in many cancers and their ATPase activity is crucial for cancer cell proliferation and the human RuvBs have been proposed as suitable drug target for cancer. Similarly one of the Plasmodium falciparum RuvB like protein (PfRuvB3) has been found to be specific to the stage where nuclear division led multiplication of parasite take place. Considering all these it seems that the R2TP complex may be playing some critical role both in the cancer cell proliferation in human and rapid multiplication of the parasites Leishmania donovani and Plasmodium falciparum. Landes Bioscience 2013-11-01 2013-08-06 /pmc/articles/PMC3913666/ /pubmed/24505500 http://dx.doi.org/10.4161/cib.26005 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Research Paper Ahmad, Moaz Afrin, Farhat Tuteja, Renu Identification of R2TP complex of Leishmania donovaniand Plasmodium falciparum using genome wide in-silico analysis |
title | Identification of R2TP complex of Leishmania donovaniand Plasmodium falciparum using genome wide in-silico analysis |
title_full | Identification of R2TP complex of Leishmania donovaniand Plasmodium falciparum using genome wide in-silico analysis |
title_fullStr | Identification of R2TP complex of Leishmania donovaniand Plasmodium falciparum using genome wide in-silico analysis |
title_full_unstemmed | Identification of R2TP complex of Leishmania donovaniand Plasmodium falciparum using genome wide in-silico analysis |
title_short | Identification of R2TP complex of Leishmania donovaniand Plasmodium falciparum using genome wide in-silico analysis |
title_sort | identification of r2tp complex of leishmania donovaniand plasmodium falciparum using genome wide in-silico analysis |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3913666/ https://www.ncbi.nlm.nih.gov/pubmed/24505500 http://dx.doi.org/10.4161/cib.26005 |
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