Project description:Pyrocystis lunula (Schutt) is a photoautotrophic unarmoured dinoflagellate, commonly found in marine environments. Today it exist several biotechnological applications derived from the bioluminescent system of this species. From a post-genomic perspective, and in order to study the whole proteome of P. lunula, a ¨omic¨ approach (transcriptomic-proteomic analysis) was initiated using fresh microalgae samples. A total of 80.875.390 reads were generated (400.000 conting, XXX pb) and 17.461 peptides were detected, getting 3.182 protein identification hits. The identified proteins were categorized according to functional description and gene ontology classification. In this study, it has been developed and described the first proteomic analysis of the microalgae P. lunula. In addition to shed light on a series of important factors involved with the processes of regulation of gene expression. The presence of the luciferin-binding protein (LBP), which had not been described so far in Pyrocystis, is highlighted.
Project description:Pyrocystis lunula is a unicellular bioluminescing dinoflagellates. While the mechanisms and genes underlying bioluminescence and luciferase synthesis are understood in many bioluminescing clades, it remains unknown in dinoflagellates. We took advantage of merging long and short reads to provide here a de novo assembly of P. lunula transcriptome. A total of 975 million filtered paired-end reads were obtained and assembled into 155,716 contigs corresponding to putative transcripts that were functionally annotated. This dataset will be valuable for improving our understanding of protist's biology and is accessible via NCBI BioProject (PRJNA727555).
Project description:Pyrocystis lunula is considered a model organism due to its bioluminescence capacity linked to circadian rhythms. The mechanisms underlying the bioluminescent phenomenon have been well characterized in dinoflagellates; however, there are still some aspects that remain an enigma. Such is the case of the presence and diversity of the luciferin-binding protein (LBP), as well as the synthesis process of luciferin. Here we carry out a review of the literature in relation to the molecular players responsible for bioluminescence in dinoflagellates, with particular interest in P. lunula. We also carried out a phylogenetic analysis of the conservation of protein sequence, structure and evolutionary pattern of these key players. The basic structure of the luciferase (LCF) is quite conserved among the sequences reported to date for dinoflagellate species, but not in the case of the LBP, which has proven to be more variable in terms of sequence and structure. In the case of luciferin, its synthesis has been shown to be complex process with more than one metabolic pathway involved. The glutathione S-transferase (GST) and the P630 or blue compound, seem to be involved in this process. In the same way, various hypotheses regarding the role of bioluminescence in dinoflagellates are exposed.