
Comparative study of lectin domains in model species : new insights into evolutionary dynamics
- Author
- Sofie Van Holle (UGent) , Kristof De Schutter (UGent) , Lore Eggermont (UGent) , Mariya Tsankova Tsaneva (UGent) , Liuyi Dang (UGent) and Els Van Damme (UGent)
- Organization
- Abstract
- Lectins are present throughout the plant kingdom and are reported to be involved in diverse biological processes. In this study, we provide a comparative analysis of the lectin families from model species in a phylogenetic framework. The analysis focuses on the different plant lectin domains identified in five representative core angiosperm genomes (Arabidopsisthaliana, Glycine max, Cucumis sativus, Oryza sativa ssp. japonica and Oryza sativa ssp. indica). The genomes were screened for genes encoding lectin domains using a combination of Basic Local Alignment Search Tool (BLAST), hidden Markov models, and InterProScan analysis. Additionally, phylogenetic relationships were investigated by constructing maximum likelihood phylogenetic trees. The results demonstrate that the majority of the lectin families are present in each of the species under study. Domain organization analysis showed that most identified proteins are multi-domain proteins, owing to the modular rearrangement of protein domains during evolution. Most of these multi-domain proteins are widespread, while others display a lineage-specific distribution. Furthermore, the phylogenetic analyses reveal that some lectin families evolved to be similar to the phylogeny of the plant species, while others share a closer evolutionary history based on the corresponding protein domain architecture. Our results yield insights into the evolutionary relationships and functional divergence of plant lectins.
- Keywords
- RECEPTOR-LIKE KINASE, RIBOSOME-INACTIVATING PROTEINS, SOYBEAN, GLYCINE-MAX, GENE COEXPRESSION NETWORKS, DISEASE RESISTANCE GENES, MANNOSE-BINDING LECTIN, JACALIN-RELATED LECTIN, CUCUMIS-SATIVUS L, PLANT-CELL DEATH, ARABIDOPSIS-THALIANA, lectin, carbohydrate, evolution, phylogeny, protein domain
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-8546387
- MLA
- Van Holle, Sofie, et al. “Comparative Study of Lectin Domains in Model Species : New Insights into Evolutionary Dynamics.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 18, no. 6, 2017, doi:10.3390/ijms18061136.
- APA
- Van Holle, S., De Schutter, K., Eggermont, L., Tsaneva, M. T., Dang, L., & Van Damme, E. (2017). Comparative study of lectin domains in model species : new insights into evolutionary dynamics. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 18(6). https://doi.org/10.3390/ijms18061136
- Chicago author-date
- Van Holle, Sofie, Kristof De Schutter, Lore Eggermont, Mariya Tsankova Tsaneva, Liuyi Dang, and Els Van Damme. 2017. “Comparative Study of Lectin Domains in Model Species : New Insights into Evolutionary Dynamics.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 18 (6). https://doi.org/10.3390/ijms18061136.
- Chicago author-date (all authors)
- Van Holle, Sofie, Kristof De Schutter, Lore Eggermont, Mariya Tsankova Tsaneva, Liuyi Dang, and Els Van Damme. 2017. “Comparative Study of Lectin Domains in Model Species : New Insights into Evolutionary Dynamics.” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 18 (6). doi:10.3390/ijms18061136.
- Vancouver
- 1.Van Holle S, De Schutter K, Eggermont L, Tsaneva MT, Dang L, Van Damme E. Comparative study of lectin domains in model species : new insights into evolutionary dynamics. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 2017;18(6).
- IEEE
- [1]S. Van Holle, K. De Schutter, L. Eggermont, M. T. Tsaneva, L. Dang, and E. Van Damme, “Comparative study of lectin domains in model species : new insights into evolutionary dynamics,” INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, vol. 18, no. 6, 2017.
@article{8546387, abstract = {{Lectins are present throughout the plant kingdom and are reported to be involved in diverse biological processes. In this study, we provide a comparative analysis of the lectin families from model species in a phylogenetic framework. The analysis focuses on the different plant lectin domains identified in five representative core angiosperm genomes (Arabidopsisthaliana, Glycine max, Cucumis sativus, Oryza sativa ssp. japonica and Oryza sativa ssp. indica). The genomes were screened for genes encoding lectin domains using a combination of Basic Local Alignment Search Tool (BLAST), hidden Markov models, and InterProScan analysis. Additionally, phylogenetic relationships were investigated by constructing maximum likelihood phylogenetic trees. The results demonstrate that the majority of the lectin families are present in each of the species under study. Domain organization analysis showed that most identified proteins are multi-domain proteins, owing to the modular rearrangement of protein domains during evolution. Most of these multi-domain proteins are widespread, while others display a lineage-specific distribution. Furthermore, the phylogenetic analyses reveal that some lectin families evolved to be similar to the phylogeny of the plant species, while others share a closer evolutionary history based on the corresponding protein domain architecture. Our results yield insights into the evolutionary relationships and functional divergence of plant lectins.}}, articleno = {{1136}}, author = {{Van Holle, Sofie and De Schutter, Kristof and Eggermont, Lore and Tsaneva, Mariya Tsankova and Dang, Liuyi and Van Damme, Els}}, issn = {{1422-0067}}, journal = {{INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES}}, keywords = {{RECEPTOR-LIKE KINASE,RIBOSOME-INACTIVATING PROTEINS,SOYBEAN,GLYCINE-MAX,GENE COEXPRESSION NETWORKS,DISEASE RESISTANCE GENES,MANNOSE-BINDING LECTIN,JACALIN-RELATED LECTIN,CUCUMIS-SATIVUS L,PLANT-CELL DEATH,ARABIDOPSIS-THALIANA,lectin,carbohydrate,evolution,phylogeny,protein domain}}, language = {{eng}}, number = {{6}}, pages = {{29}}, title = {{Comparative study of lectin domains in model species : new insights into evolutionary dynamics}}, url = {{http://doi.org/10.3390/ijms18061136}}, volume = {{18}}, year = {{2017}}, }
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