LIP4 Is Involved in Triacylglycerol Degradation in Chlamydomonas reinhardtii.
Chlamydomonas reinhardtii
Lipid catabolism
N resupply
SUGAR DEPENDENT1
Triacylglycerol degradation
Triacylglycerol lipase
Journal
Plant & cell physiology
ISSN: 1471-9053
Titre abrégé: Plant Cell Physiol
Pays: Japan
ID NLM: 9430925
Informations de publication
Date de publication:
01 Jun 2019
01 Jun 2019
Historique:
received:
30
11
2018
accepted:
13
02
2019
pubmed:
24
2
2019
medline:
2
8
2019
entrez:
24
2
2019
Statut:
ppublish
Résumé
Degradation of the storage compound triacylglycerol (TAG) is a crucial process in response to environmental stimuli. In microalgae, this process is important for re-growth when conditions become favorable after cells have experienced stresses. Mobilization of TAG is initiated by actions of lipases causing the release of glycerol and free fatty acids, which can be further broken down for energy production or recycled to synthesize membrane lipids. Although key enzymes in the process, TAG lipases remain to be characterized in the model green alga Chlamydomonas reinhardtii. Here, we describe the functional analysis of a putative TAG lipase, i.e. LIP4, which shares 44% amino acid identity with the major TAG lipase in Arabidopsis (SUGAR DEPENDENT1-SDP1). The LIP4 transcript level was downregulated during nitrogen deprivation when TAG accumulates, but was upregulated during nitrogen resupply (NR) when TAG was degraded. Both artificial microRNA and insertional mutants showed a delay in TAG mobilization during NR. The difference in TAG degradation was more pronounced when the cultures were incubated without acetate in the dark. Furthermore, the lip4 insertional mutants over-accumulated TAG during optimal growth conditions. Taken together, the results suggest to us that LIP4 likely acts as a TAG lipase and plays a role in TAG homeostasis in Chlamydomonas.
Identifiants
pubmed: 30796452
pii: 5362038
doi: 10.1093/pcp/pcz037
doi:
Substances chimiques
Algal Proteins
0
Arabidopsis Proteins
0
Triglycerides
0
Carboxylic Ester Hydrolases
EC 3.1.1.-
Lipase
EC 3.1.1.3
SDP1 protein, Arabidopsis
EC 3.1.1.3
Types de publication
Journal Article
Langues
eng
Pagination
1250-1259Informations de copyright
� The Author(s) 2019. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oup.com.