Analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway

Background: Microalgal triglyceride (TAG) synthesis has attracted considerable attention. Particular emphasis has been put towards characterizing the algal homologs of the canonical rate-limiting enzymes, diacylglycerol acyltransferase (DGAT) and phospholipid:diacylglycerol acyltransferase (PDAT). L...

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Detalles Bibliográficos
Autores principales: Bagnato, C., Prados, M.B., Franchini, G.R., Scaglia, N., Miranda, S.E., Beligni, M.V.
Formato: JOUR
Materias:
Algae
Biodiesel production
Chloroplast
HMMER profiling
Neutral lipids
Protein phylogeny
Soluble acyltransferase
Triglyceride metabolism
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_14712164_v18_n1_p_Bagnato
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_14712164_v18_n1_p_Bagnato
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spelling todo:paper_14712164_v18_n1_p_Bagnato2023-10-03T16:17:47Z Analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway Bagnato, C. Prados, M.B. Franchini, G.R. Scaglia, N. Miranda, S.E. Beligni, M.V. Algae Biodiesel production Chloroplast HMMER profiling Neutral lipids Protein phylogeny Soluble acyltransferase Triglyceride metabolism Background: Microalgal triglyceride (TAG) synthesis has attracted considerable attention. Particular emphasis has been put towards characterizing the algal homologs of the canonical rate-limiting enzymes, diacylglycerol acyltransferase (DGAT) and phospholipid:diacylglycerol acyltransferase (PDAT). Less work has been done to analyze homologs from a phylogenetic perspective. In this work, we used HMMER iterative profiling and phylogenetic and functional analyses to determine the number and sequence characteristics of algal DGAT and PDAT, as well as related sequences that constitute their corresponding superfamilies. We included most algae with available genomes, as well as representative eukaryotic and prokaryotic species. Results: Amongst our main findings, we identified a novel clade of DGAT1-like proteins exclusive to red algae and glaucophyta and a previously uncharacterized subclade of DGAT2 proteins with an unusual number of transmembrane segments. Our analysis also revealed the existence of a novel DGAT exclusive to green algae with moderate similarity to plant soluble DGAT3. The DGAT3 clade shares a most recent ancestor with a group of uncharacterized proteins from cyanobacteria. Subcellular targeting prediction suggests that most green algal DGAT3 proteins are imported to the chloroplast, evidencing that the green algal chloroplast might have a soluble pathway for the de novo synthesis of TAGs. Heterologous expression of C. reinhardtii DGAT3 produces an increase in the accumulation of TAG, as evidenced by thin layer chromatography. Conclusions: Our analysis contributes to advance in the knowledge of complex superfamilies involved in lipid metabolism and provides clues to possible enzymatic players of chloroplast TAG synthesis. © 2017 The Author(s). JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_14712164_v18_n1_p_Bagnato
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Algae
Biodiesel production
Chloroplast
HMMER profiling
Neutral lipids
Protein phylogeny
Soluble acyltransferase
Triglyceride metabolism
spellingShingle Algae
Biodiesel production
Chloroplast
HMMER profiling
Neutral lipids
Protein phylogeny
Soluble acyltransferase
Triglyceride metabolism
Bagnato, C.
Prados, M.B.
Franchini, G.R.
Scaglia, N.
Miranda, S.E.
Beligni, M.V.
Analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway
topic_facet Algae
Biodiesel production
Chloroplast
HMMER profiling
Neutral lipids
Protein phylogeny
Soluble acyltransferase
Triglyceride metabolism
description Background: Microalgal triglyceride (TAG) synthesis has attracted considerable attention. Particular emphasis has been put towards characterizing the algal homologs of the canonical rate-limiting enzymes, diacylglycerol acyltransferase (DGAT) and phospholipid:diacylglycerol acyltransferase (PDAT). Less work has been done to analyze homologs from a phylogenetic perspective. In this work, we used HMMER iterative profiling and phylogenetic and functional analyses to determine the number and sequence characteristics of algal DGAT and PDAT, as well as related sequences that constitute their corresponding superfamilies. We included most algae with available genomes, as well as representative eukaryotic and prokaryotic species. Results: Amongst our main findings, we identified a novel clade of DGAT1-like proteins exclusive to red algae and glaucophyta and a previously uncharacterized subclade of DGAT2 proteins with an unusual number of transmembrane segments. Our analysis also revealed the existence of a novel DGAT exclusive to green algae with moderate similarity to plant soluble DGAT3. The DGAT3 clade shares a most recent ancestor with a group of uncharacterized proteins from cyanobacteria. Subcellular targeting prediction suggests that most green algal DGAT3 proteins are imported to the chloroplast, evidencing that the green algal chloroplast might have a soluble pathway for the de novo synthesis of TAGs. Heterologous expression of C. reinhardtii DGAT3 produces an increase in the accumulation of TAG, as evidenced by thin layer chromatography. Conclusions: Our analysis contributes to advance in the knowledge of complex superfamilies involved in lipid metabolism and provides clues to possible enzymatic players of chloroplast TAG synthesis. © 2017 The Author(s).
format JOUR
author Bagnato, C.
Prados, M.B.
Franchini, G.R.
Scaglia, N.
Miranda, S.E.
Beligni, M.V.
author_facet Bagnato, C.
Prados, M.B.
Franchini, G.R.
Scaglia, N.
Miranda, S.E.
Beligni, M.V.
author_sort Bagnato, C.
title Analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway
title_short Analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway
title_full Analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway
title_fullStr Analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway
title_full_unstemmed Analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway
title_sort analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway
url http://hdl.handle.net/20.500.12110/paper_14712164_v18_n1_p_Bagnato
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