Cargando…
Comparative analysis of fungal protein kinases and associated domains
BACKGROUND: Protein phosphorylation is responsible for a large portion of the regulatory functions of eukaryotic cells. Although the list of sequenced genomes of filamentous fungi has grown rapidly, the kinomes of recently sequenced species have not yet been studied in detail. The objective of this...
Autores principales: | , , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838846/ https://www.ncbi.nlm.nih.gov/pubmed/20178650 http://dx.doi.org/10.1186/1471-2164-11-133 |
_version_ | 1782178899424182272 |
---|---|
author | Kosti, Idit Mandel-Gutfreund, Yael Glaser, Fabian Horwitz, Benjamin A |
author_facet | Kosti, Idit Mandel-Gutfreund, Yael Glaser, Fabian Horwitz, Benjamin A |
author_sort | Kosti, Idit |
collection | PubMed |
description | BACKGROUND: Protein phosphorylation is responsible for a large portion of the regulatory functions of eukaryotic cells. Although the list of sequenced genomes of filamentous fungi has grown rapidly, the kinomes of recently sequenced species have not yet been studied in detail. The objective of this study is to apply a comparative analysis of the kinase distribution in different fungal phyla, and to explore its relevance to understanding the evolution of fungi and their taxonomic classification. We have analyzed in detail 12 subgroups of kinases and their distribution over 30 species, as well as their potential use as a classifier for members of the fungal kingdom. RESULTS: Our findings show that despite the similarity of the kinase distribution in all fungi, their domain distributions and kinome density can potentially be used to classify them and give insight into their evolutionary origin. In general, we found that the overall representation of kinase groups is similar across fungal genomes, the only exception being a large number of tyrosine kinase-like (TKL) kinases predicted in Laccaria bicolor. This unexpected finding underscores the need to continue to sequence fungal genomes, since many species or lineage-specific properties may remain to be discovered. Furthermore, we found that the domain organization significantly varies between the fungal species. Our results suggest that protein kinases and their functional domains strongly reflect fungal taxonomy. CONCLUSIONS: Comparison of the predicted kinomes of sequenced fungi suggests essential signaling functions common to all species, but also specific adaptations of the signal transduction networks to particular species. |
format | Text |
id | pubmed-2838846 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-28388462010-03-16 Comparative analysis of fungal protein kinases and associated domains Kosti, Idit Mandel-Gutfreund, Yael Glaser, Fabian Horwitz, Benjamin A BMC Genomics Research Article BACKGROUND: Protein phosphorylation is responsible for a large portion of the regulatory functions of eukaryotic cells. Although the list of sequenced genomes of filamentous fungi has grown rapidly, the kinomes of recently sequenced species have not yet been studied in detail. The objective of this study is to apply a comparative analysis of the kinase distribution in different fungal phyla, and to explore its relevance to understanding the evolution of fungi and their taxonomic classification. We have analyzed in detail 12 subgroups of kinases and their distribution over 30 species, as well as their potential use as a classifier for members of the fungal kingdom. RESULTS: Our findings show that despite the similarity of the kinase distribution in all fungi, their domain distributions and kinome density can potentially be used to classify them and give insight into their evolutionary origin. In general, we found that the overall representation of kinase groups is similar across fungal genomes, the only exception being a large number of tyrosine kinase-like (TKL) kinases predicted in Laccaria bicolor. This unexpected finding underscores the need to continue to sequence fungal genomes, since many species or lineage-specific properties may remain to be discovered. Furthermore, we found that the domain organization significantly varies between the fungal species. Our results suggest that protein kinases and their functional domains strongly reflect fungal taxonomy. CONCLUSIONS: Comparison of the predicted kinomes of sequenced fungi suggests essential signaling functions common to all species, but also specific adaptations of the signal transduction networks to particular species. BioMed Central 2010-02-24 /pmc/articles/PMC2838846/ /pubmed/20178650 http://dx.doi.org/10.1186/1471-2164-11-133 Text en Copyright ©2010 Kosti 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 Kosti, Idit Mandel-Gutfreund, Yael Glaser, Fabian Horwitz, Benjamin A Comparative analysis of fungal protein kinases and associated domains |
title | Comparative analysis of fungal protein kinases and associated domains |
title_full | Comparative analysis of fungal protein kinases and associated domains |
title_fullStr | Comparative analysis of fungal protein kinases and associated domains |
title_full_unstemmed | Comparative analysis of fungal protein kinases and associated domains |
title_short | Comparative analysis of fungal protein kinases and associated domains |
title_sort | comparative analysis of fungal protein kinases and associated domains |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838846/ https://www.ncbi.nlm.nih.gov/pubmed/20178650 http://dx.doi.org/10.1186/1471-2164-11-133 |
work_keys_str_mv | AT kostiidit comparativeanalysisoffungalproteinkinasesandassociateddomains AT mandelgutfreundyael comparativeanalysisoffungalproteinkinasesandassociateddomains AT glaserfabian comparativeanalysisoffungalproteinkinasesandassociateddomains AT horwitzbenjamina comparativeanalysisoffungalproteinkinasesandassociateddomains |