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Monogalactosyldiacylglycerol and Sulfolipid Synthesis in Microalgae

Microalgae, due to their huge taxonomic and metabolic diversity, have been shown to be a valuable and eco-friendly source of bioactive natural products. The increasing number of genomic and transcriptomic data will give a great boost for the study of metabolic pathways involved in the synthesis of b...

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Autores principales: Riccio, Gennaro, De Luca, Daniele, Lauritano, Chiara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7281551/
https://www.ncbi.nlm.nih.gov/pubmed/32370033
http://dx.doi.org/10.3390/md18050237
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author Riccio, Gennaro
De Luca, Daniele
Lauritano, Chiara
author_facet Riccio, Gennaro
De Luca, Daniele
Lauritano, Chiara
author_sort Riccio, Gennaro
collection PubMed
description Microalgae, due to their huge taxonomic and metabolic diversity, have been shown to be a valuable and eco-friendly source of bioactive natural products. The increasing number of genomic and transcriptomic data will give a great boost for the study of metabolic pathways involved in the synthesis of bioactive compounds. In this study, we analyzed the presence of the enzymes involved in the synthesis of monogalactosyldiacylglycerols (MGDGs) and sulfoquinovosyldiacylglycerols (SQDG). Both compounds have important biological properties. MGDGs present both anti-inflammatory and anti-cancer activities while SQDGs present immunostimulatory activities and inhibit the enzyme glutaminyl cyclase, which is involved in Alzheimer’s disease. The Ocean Global Atlas (OGA) database and the Marine Microbial Eukaryotic Transcriptome Sequencing Project (MMETSP) were used to search MGDG synthase (MGD), UDP-sulfoquinovose synthase (SQD1), and sulfoquinovosyltransferase (SQD2) sequences along microalgal taxa. In silico 3D prediction analyses for the three enzymes were performed by Phyre2 server, while binding site predictions were performed by the COACH server. The analyzed enzymes are distributed across different taxa, which confirms the importance for microalgae of these two pathways for thylakoid physiology. MGD genes have been found across almost all analyzed taxa and can be separated in two different groups, similarly to terrestrial plant MGD. SQD1 and SQD2 genes are widely distributed along the analyzed taxa in a similar way to MGD genes with some exceptions. For Pinguiophyceae, Raphidophyceae, and Synurophyceae, only sequences coding for MGDG were found. On the contrary, sequences assigned to Ciliophora and Eustigmatophyceae were exclusively corresponding to SQD1 and SQD2. This study reports, for the first time, the presence/absence of these enzymes in available microalgal transcriptomes, which gives new insights on microalgal physiology and possible biotechnological applications for the production of bioactive lipids.
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spelling pubmed-72815512020-06-17 Monogalactosyldiacylglycerol and Sulfolipid Synthesis in Microalgae Riccio, Gennaro De Luca, Daniele Lauritano, Chiara Mar Drugs Article Microalgae, due to their huge taxonomic and metabolic diversity, have been shown to be a valuable and eco-friendly source of bioactive natural products. The increasing number of genomic and transcriptomic data will give a great boost for the study of metabolic pathways involved in the synthesis of bioactive compounds. In this study, we analyzed the presence of the enzymes involved in the synthesis of monogalactosyldiacylglycerols (MGDGs) and sulfoquinovosyldiacylglycerols (SQDG). Both compounds have important biological properties. MGDGs present both anti-inflammatory and anti-cancer activities while SQDGs present immunostimulatory activities and inhibit the enzyme glutaminyl cyclase, which is involved in Alzheimer’s disease. The Ocean Global Atlas (OGA) database and the Marine Microbial Eukaryotic Transcriptome Sequencing Project (MMETSP) were used to search MGDG synthase (MGD), UDP-sulfoquinovose synthase (SQD1), and sulfoquinovosyltransferase (SQD2) sequences along microalgal taxa. In silico 3D prediction analyses for the three enzymes were performed by Phyre2 server, while binding site predictions were performed by the COACH server. The analyzed enzymes are distributed across different taxa, which confirms the importance for microalgae of these two pathways for thylakoid physiology. MGD genes have been found across almost all analyzed taxa and can be separated in two different groups, similarly to terrestrial plant MGD. SQD1 and SQD2 genes are widely distributed along the analyzed taxa in a similar way to MGD genes with some exceptions. For Pinguiophyceae, Raphidophyceae, and Synurophyceae, only sequences coding for MGDG were found. On the contrary, sequences assigned to Ciliophora and Eustigmatophyceae were exclusively corresponding to SQD1 and SQD2. This study reports, for the first time, the presence/absence of these enzymes in available microalgal transcriptomes, which gives new insights on microalgal physiology and possible biotechnological applications for the production of bioactive lipids. MDPI 2020-05-01 /pmc/articles/PMC7281551/ /pubmed/32370033 http://dx.doi.org/10.3390/md18050237 Text en © 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/).
spellingShingle Article
Riccio, Gennaro
De Luca, Daniele
Lauritano, Chiara
Monogalactosyldiacylglycerol and Sulfolipid Synthesis in Microalgae
title Monogalactosyldiacylglycerol and Sulfolipid Synthesis in Microalgae
title_full Monogalactosyldiacylglycerol and Sulfolipid Synthesis in Microalgae
title_fullStr Monogalactosyldiacylglycerol and Sulfolipid Synthesis in Microalgae
title_full_unstemmed Monogalactosyldiacylglycerol and Sulfolipid Synthesis in Microalgae
title_short Monogalactosyldiacylglycerol and Sulfolipid Synthesis in Microalgae
title_sort monogalactosyldiacylglycerol and sulfolipid synthesis in microalgae
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7281551/
https://www.ncbi.nlm.nih.gov/pubmed/32370033
http://dx.doi.org/10.3390/md18050237
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