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      New Perspectives Related to the Bioluminescent System in Dinoflagellates: Pyrocystis lunula, a Case Study

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          Abstract

          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.

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          Bioluminescence in the sea.

          Bioluminescence spans all oceanic dimensions and has evolved many times--from bacteria to fish--to powerfully influence behavioral and ecosystem dynamics. New methods and technology have brought great advances in understanding of the molecular basis of bioluminescence, its physiological control, and its significance in marine communities. Novel tools derived from understanding the chemistry of natural light-producing molecules have led to countless valuable applications, culminating recently in a related Nobel Prize. Marine organisms utilize bioluminescence for vital functions ranging from defense to reproduction. To understand these interactions and the distributions of luminous organisms, new instruments and platforms allow observations on individual to oceanographic scales. This review explores recent advances, including the chemical and molecular, phylogenetic and functional, community and oceanographic aspects of bioluminescence.
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            Bioluminescence.

            Bioluminescence has evolved independently many times; thus the responsible genes are unrelated in bacteria, unicellular algae, coelenterates, beetles, fishes, and others. Chemically, all involve exergonic reactions of molecular oxygen with different substrates (luciferins) and enzymes (luciferases), resulting in photons of visible light (approximately 50 kcal). In addition to the structure of luciferan, several factors determine the color of the emissions, such as the amino acid sequence of the luciferase (as in beetles, for example) or the presence of accessory proteins, notably GFP, discovered in coelenterates and now used as a reporter of gene expression and a cellular marker. The mechanisms used to control the intensity and kinetics of luminescence, often emitted as flashes, also vary. Bioluminescence is credited with the discovery of how some bacteria, luminous or not, sense their density and regulate specific genes by chemical communication, as in the fascinating example of symbiosis between luminous bacteria and squid.
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              Glutathione transferases in bacteria.

              Bacterial glutathione transferases (GSTs) are part of a superfamily of enzymes that play a key role in cellular detoxification. GSTs are widely distributed in prokaryotes and are grouped into several classes. Bacterial GSTs are implicated in a variety of distinct processes such as the biodegradation of xenobiotics, protection against chemical and oxidative stresses and antimicrobial drug resistance. In addition to their role in detoxification, bacterial GSTs are also involved in a variety of distinct metabolic processes such as the biotransformation of dichloromethane, the degradation of lignin and atrazine, and the reductive dechlorination of pentachlorophenol. This review article summarizes the current status of knowledge regarding the functional and structural properties of bacterial GSTs.
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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                05 March 2020
                March 2020
                : 21
                : 5
                : 1784
                Affiliations
                [1 ]Microbiology Laboratory, Institute of Viticulture and Agri-food Research (IVAGRO), Environmental and Marine Sciences Faculty. University of Cadiz (UCA), 11510 Puerto Real, Spain; carfaqui07@ 123456yahoo.es
                [2 ]Tecnologico de Monterrey, Escuela de Ingenieria y Ciencias, 76130 Queretaro, Mexico; mdedonate@ 123456tec.mx (M.D.D.); herodulfo@ 123456tec.mx (H.R.)
                [3 ]Institute of Marine Sciences of Andalusia (ICMAN), Department of Marine Biology and Aquaculture, Spanish National Research Council (CSIC), 11519 Puerto Real, Spain; gonzalo.martinez@ 123456csic.es
                [4 ]Interdisciplinary Centre of Marine and Environmental Research of the University of Porto (CIIMAR), 4450-208 Matosinhos, Portugal; bcostas@ 123456ciimar.up.pt
                [5 ]Institute of Biomedical Sciences Abel Salazar (ICBAS-UP), University of Porto, 4050-313 Porto, Portugal
                [6 ]Faculty of Marine and Environmental Sciences, Biology Department, University of Cadiz (UCA), 11510 Puerto Real, Spain; juanmiguel.mancera@ 123456uca.es
                Author notes
                Author information
                https://orcid.org/0000-0001-9403-2211
                https://orcid.org/0000-0001-8860-6020
                https://orcid.org/0000-0003-3758-0849
                https://orcid.org/0000-0003-0751-5966
                https://orcid.org/0000-0002-4052-6141
                Article
                ijms-21-01784
                10.3390/ijms21051784
                7084563
                32150894
                4ee5c462-b480-4575-9b9a-ded2c3e9ea7a
                © 2020 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 27 January 2020
                : 03 March 2020
                Categories
                Review

                Molecular biology
                luciferase,luciferin-binding protein,luciferin,p630,blue compound,glutathione s-transferase

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