BBX proteins in green plants insights into their evolution, structure, feature and functional diversification
The B-box domain is conserved in a large number of proteins involved in cell growth control, differentiation and transcriptional regulation among animal and plant species. In Arabidopsis thaliana, some works have found that B-box proteins [BBX] play central developmental functions in flowering, light and abiotic stress signaling. Despite the functional importance of this protein family, evolutionary and structural relationships of BBX proteins have not been extensively investigated in the plant kingdom. Using a phylogenetic approach, we conducted a comprehensive evolutionary analysis of the BBX protein family in twelve plant species [four green algae, one moss, one lycophyte, three monocots and three dicots]. The analysis classified 214 BBX proteins into five structure groups, which evolved independently at early stages of green plant evolution. We showed that the B-box consensus sequences of each structure groups retained a common and conserved domain topology. Furthermore, we identified seven novel motifs specific to each structure group and a valine-proline [VP] pair conserved at the C-terminus domain in some BBX proteins suggesting that they are required for protein-protein interactions. As it has been documented in mammalian systems, we also found monopartite and bipartite amino acid sequences at the C-terminus domain that could function as nuclear localization signals [NLSs]. The five BBX structure groups evolved constrained by the conservation of amino acid sequences in the two B-boxes, but radiating variation into NLSs and novel motifs of each structural group. We suggest that these features are the functional basis for the BBX protein diversity in green plants.
| Main Authors: | , |
|---|---|
| Format: | Texto biblioteca |
| Language: | eng |
| Subjects: | B-BOX DOMAINS, BBX PROTEINS, CCT DOMAIN, NUCLEAR LOCALIZATION SIGNALS [NLSS], PLANT EVOLUTION, VEGETABLE PROTEIN, AMINO ACID SEQUENCE, ANGIOSPERM, CONSENSUS SEQUENCE, EVOLUTION, GREEN ALGA, MONOCOT, MOSS, NONHUMAN, NUCLEAR LOCALIZATION SIGNAL, PHYLOGENETIC TREE, PHYLOGENY, PLANT GENOME, PROTEIN FAMILY, PROTEIN FUNCTION, PROTEIN PROTEIN INTERACTION, PROTEIN STRUCTURE, SPECIES, VIRIDIPLANTAE, VALINE-PROLINE, VP, CONSERVED SEQUENCE, DNA-BINDING PROTEINS, EVOLUTION, MOLECULAR, MOLECULAR SEQUENCE DATA, MULTIGENE FAMILY, PLANT PROTEINS, POSITION-SPECIFIC SCORING MATRICES, PROTEIN INTERACTION DOMAINS AND MOTIFS, ANIMALIA, ARABIDOPSIS THALIANA, BRYOPHYTA, CHLOROPHYTA, DICOTYLEDONEAE, LILIOPSIDA, MAMMALIA, CO-LIKE, COL, CONSTANS, NLS, AMINO ACID MOTIFS, |
| Online Access: | http://ceiba.agro.uba.ar/cgi-bin/koha/opac-detail.pl?biblionumber=46887 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Summary: | The B-box domain is conserved in a large number of proteins involved in cell growth control, differentiation and transcriptional regulation among animal and plant species. In Arabidopsis thaliana, some works have found that B-box proteins [BBX] play central developmental functions in flowering, light and abiotic stress signaling. Despite the functional importance of this protein family, evolutionary and structural relationships of BBX proteins have not been extensively investigated in the plant kingdom. Using a phylogenetic approach, we conducted a comprehensive evolutionary analysis of the BBX protein family in twelve plant species [four green algae, one moss, one lycophyte, three monocots and three dicots]. The analysis classified 214 BBX proteins into five structure groups, which evolved independently at early stages of green plant evolution. We showed that the B-box consensus sequences of each structure groups retained a common and conserved domain topology. Furthermore, we identified seven novel motifs specific to each structure group and a valine-proline [VP] pair conserved at the C-terminus domain in some BBX proteins suggesting that they are required for protein-protein interactions. As it has been documented in mammalian systems, we also found monopartite and bipartite amino acid sequences at the C-terminus domain that could function as nuclear localization signals [NLSs]. The five BBX structure groups evolved constrained by the conservation of amino acid sequences in the two B-boxes, but radiating variation into NLSs and novel motifs of each structural group. We suggest that these features are the functional basis for the BBX protein diversity in green plants. |
|---|