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

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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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Autor principal: Bagnato, C.
Otros Autores: Prados, M.B, Franchini, G.R, Scaglia, N., Miranda, S.E, Beligni, M.V
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: BioMed Central Ltd. 2017
Acceso en línea:Registro en Scopus
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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100 1 |a Bagnato, C. 
245 1 0 |a Analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway 
260 |b BioMed Central Ltd.  |c 2017 
270 1 0 |m Beligni, M.V.; Instituto de Investigaciones Biológicas (IIB-CONICET-UNMdP), Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata, CC 1245, Argentina; email: mvbeligni@mdp.edu.ar 
506 |2 openaire  |e Política editorial 
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520 3 |a 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).  |l eng 
536 |a Detalles de la financiación: PICT-2013-2122, ANPCyT, Agencia Nacional de Promoción Científica y Tecnológica 
536 |a Detalles de la financiación: We thank Dr. Matías Mora for providing an evolutionary perspective to our DGAT3 results. We also thank Dr. Héctor Alvarez for critical input on our TLC analyses.This work was supported by funds to MVB from the Argentinean Consejo Nacional de Investigaciones Científicas y Tecnológicas (CONICET-PIP 11420110100090) and from Agencia Nacional de Promoción Científica y Tecnológica (ANPCyT, PICT-2013-2122). MVB, CB, MBP, GRF, NS and SEM are CONICET Researchers. 
593 |a Instituto de Energía y Desarrollo Sustentable, Comisión Nacional de Energía Atómica, Centro Atómico Bariloche, Av. Bustillo 9500, 8400S. C. de Bariloche, Río Negro, Argentina 
593 |a Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP-CONICET-UNLP), Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Calle 60 y 120 s/n, La Plata, Argentina 
593 |a Universidad de Buenos Aires, CONICET Instituto de Investigaciones Cardiológicas (ININCA), Laboratorio de Glico-Inmuno-Biología, Marcelo T. de Alvear 2270, C1122AAJ, Buenos Aires, Argentina 
593 |a Instituto de Investigaciones Biológicas (IIB-CONICET-UNMdP), Facultad de Ciencias Exactas y Naturales, Universidad Nacional de Mar del Plata, CC 1245, Mar del Plata, Argentina 
690 1 0 |a ALGAE 
690 1 0 |a BIODIESEL PRODUCTION 
690 1 0 |a CHLOROPLAST 
690 1 0 |a HMMER PROFILING 
690 1 0 |a NEUTRAL LIPIDS 
690 1 0 |a PROTEIN PHYLOGENY 
690 1 0 |a SOLUBLE ACYLTRANSFERASE 
690 1 0 |a TRIGLYCERIDE METABOLISM 
700 1 |a Prados, M.B. 
700 1 |a Franchini, G.R. 
700 1 |a Scaglia, N. 
700 1 |a Miranda, S.E. 
700 1 |a Beligni, M.V. 
773 0 |d BioMed Central Ltd., 2017  |g v. 18  |k n. 1  |x 14712164  |w (AR-BaUEN)CENRE-4026  |t BMC Genomics 
856 4 1 |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-85014803832&doi=10.1186%2fs12864-017-3602-0&partnerID=40&md5=29ecb38e9d2719cb54271bdbe5a615c3  |y Registro en Scopus 
856 4 0 |u https://doi.org/10.1186/s12864-017-3602-0  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_14712164_v18_n1_p_Bagnato  |y Handle 
856 4 0 |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14712164_v18_n1_p_Bagnato  |y Registro en la Biblioteca Digital 
961 |a paper_14712164_v18_n1_p_Bagnato  |b paper  |c PE 
962 |a info:eu-repo/semantics/article  |a info:ar-repo/semantics/artículo  |b info:eu-repo/semantics/publishedVersion 
999 |c 76098 

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