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Diversity of heterotrimeric G-protein γ subunits in plants
BACKGROUND: Heterotrimeric G-proteins, consisting of three subunits Gα, Gβ and Gγ are present in most eukaryotes and mediate signaling in numerous biological processes. In plants, Gγ subunits were shown to provide functional selectivity to G-proteins. Three unconventional Gγ subunits were recently r...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3508898/ https://www.ncbi.nlm.nih.gov/pubmed/23113884 http://dx.doi.org/10.1186/1756-0500-5-608 |
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author | Trusov, Yuri Chakravorty, David Botella, José Ramón |
author_facet | Trusov, Yuri Chakravorty, David Botella, José Ramón |
author_sort | Trusov, Yuri |
collection | PubMed |
description | BACKGROUND: Heterotrimeric G-proteins, consisting of three subunits Gα, Gβ and Gγ are present in most eukaryotes and mediate signaling in numerous biological processes. In plants, Gγ subunits were shown to provide functional selectivity to G-proteins. Three unconventional Gγ subunits were recently reported in Arabidopsis, rice and soybean but no structural analysis has been reported so far. Their relationship with conventional Gγ subunits and taxonomical distribution has not been yet demonstrated. RESULTS: After an extensive similarity search through plant genomes, transcriptomes and proteomes we assembled over 200 non-redundant proteins related to the known Gγ subunits. Structural analysis of these sequences revealed that most of them lack the obligatory C-terminal prenylation motif (CaaX). According to their C-terminal structures we classified the plant Gγ subunits into three distinct types. Type A consists of Gγ subunits with a putative prenylation motif. Type B subunits lack a prenylation motif and do not have any cysteine residues in the C-terminal region, while type C subunits contain an extended C-terminal domain highly enriched with cysteines. Comparative analysis of C-terminal domains of the proteins, intron-exon arrangement of the corresponding genes and phylogenetic studies suggested a common origin of all plant Gγ subunits. CONCLUSION: Phylogenetic analyses suggest that types C and B most probably originated independently from type A ancestors. We speculate on a potential mechanism used by those Gγ subunits lacking isoprenylation motifs to anchor the Gβγ dimer to the plasma membrane and propose a new flexible nomenclature for plant Gγ subunits. Finally, in the light of our new classification, we give a word of caution about the interpretation of Gγ research in Arabidopsis and its generalization to other plant species. |
format | Online Article Text |
id | pubmed-3508898 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-35088982012-11-29 Diversity of heterotrimeric G-protein γ subunits in plants Trusov, Yuri Chakravorty, David Botella, José Ramón BMC Res Notes Research Article BACKGROUND: Heterotrimeric G-proteins, consisting of three subunits Gα, Gβ and Gγ are present in most eukaryotes and mediate signaling in numerous biological processes. In plants, Gγ subunits were shown to provide functional selectivity to G-proteins. Three unconventional Gγ subunits were recently reported in Arabidopsis, rice and soybean but no structural analysis has been reported so far. Their relationship with conventional Gγ subunits and taxonomical distribution has not been yet demonstrated. RESULTS: After an extensive similarity search through plant genomes, transcriptomes and proteomes we assembled over 200 non-redundant proteins related to the known Gγ subunits. Structural analysis of these sequences revealed that most of them lack the obligatory C-terminal prenylation motif (CaaX). According to their C-terminal structures we classified the plant Gγ subunits into three distinct types. Type A consists of Gγ subunits with a putative prenylation motif. Type B subunits lack a prenylation motif and do not have any cysteine residues in the C-terminal region, while type C subunits contain an extended C-terminal domain highly enriched with cysteines. Comparative analysis of C-terminal domains of the proteins, intron-exon arrangement of the corresponding genes and phylogenetic studies suggested a common origin of all plant Gγ subunits. CONCLUSION: Phylogenetic analyses suggest that types C and B most probably originated independently from type A ancestors. We speculate on a potential mechanism used by those Gγ subunits lacking isoprenylation motifs to anchor the Gβγ dimer to the plasma membrane and propose a new flexible nomenclature for plant Gγ subunits. Finally, in the light of our new classification, we give a word of caution about the interpretation of Gγ research in Arabidopsis and its generalization to other plant species. BioMed Central 2012-10-31 /pmc/articles/PMC3508898/ /pubmed/23113884 http://dx.doi.org/10.1186/1756-0500-5-608 Text en Copyright ©2012 Trusov 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 Trusov, Yuri Chakravorty, David Botella, José Ramón Diversity of heterotrimeric G-protein γ subunits in plants |
title | Diversity of heterotrimeric G-protein γ subunits in plants |
title_full | Diversity of heterotrimeric G-protein γ subunits in plants |
title_fullStr | Diversity of heterotrimeric G-protein γ subunits in plants |
title_full_unstemmed | Diversity of heterotrimeric G-protein γ subunits in plants |
title_short | Diversity of heterotrimeric G-protein γ subunits in plants |
title_sort | diversity of heterotrimeric g-protein γ subunits in plants |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3508898/ https://www.ncbi.nlm.nih.gov/pubmed/23113884 http://dx.doi.org/10.1186/1756-0500-5-608 |
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