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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Autores principales: Bagnato, Carolina, Prados, María B., Franchini, Gisela Raquel, Scaglia, Natalia, Miranda, Silvia E., Beligni, María E.
Formato: Articulo
Lenguaje:Inglés
Publicado: 2017
Materias:
Ciencias Médicas
Ciencias Exactas
Algae
Biodiesel production
Chloroplast
HMMER profiling
Neutral lipids
Protein phylogeny
Soluble acyltransferase
Triglyceride metabolism
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/87376
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-87376
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Médicas
Ciencias Exactas
Algae
Biodiesel production
Chloroplast
HMMER profiling
Neutral lipids
Protein phylogeny
Soluble acyltransferase
Triglyceride metabolism
spellingShingle Ciencias Médicas
Ciencias Exactas
Algae
Biodiesel production
Chloroplast
HMMER profiling
Neutral lipids
Protein phylogeny
Soluble acyltransferase
Triglyceride metabolism
Bagnato, Carolina
Prados, María B.
Franchini, Gisela Raquel
Scaglia, Natalia
Miranda, Silvia E.
Beligni, María E.
Analysis of triglyceride synthesis unveils a green algal soluble diacylglycerol acyltransferase and provides clues to potential enzymatic components of the chloroplast pathway
topic_facet Ciencias Médicas
Ciencias Exactas
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 <i>de novo</i> synthesis of TAGs. Heterologous expression of <i>C. reinhardtii</i> 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.
format Articulo
Articulo
author Bagnato, Carolina
Prados, María B.
Franchini, Gisela Raquel
Scaglia, Natalia
Miranda, Silvia E.
Beligni, María E.
author_facet Bagnato, Carolina
Prados, María B.
Franchini, Gisela Raquel
Scaglia, Natalia
Miranda, Silvia E.
Beligni, María E.
author_sort Bagnato, Carolina
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
publishDate 2017
url http://sedici.unlp.edu.ar/handle/10915/87376
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