Branched-Chain Amino Acid Catabolism Impacts Triacylglycerol Homeostasis in Chlamydomonas reinhardtii. Issue 4 (6th February 2019)
- Record Type:
- Journal Article
- Title:
- Branched-Chain Amino Acid Catabolism Impacts Triacylglycerol Homeostasis in Chlamydomonas reinhardtii. Issue 4 (6th February 2019)
- Main Title:
- Branched-Chain Amino Acid Catabolism Impacts Triacylglycerol Homeostasis in Chlamydomonas reinhardtii
- Authors:
- Liang, Yuanxue
Kong, Fantao
Torres-Romero, Ismael
Burlacot, Adrien
Cuine, Stéphan
Légeret, Bertrand
Billon, Emmanuelle
Brotman, Yariv
Alseekh, Saleh
Fernie, Alisdair R.
Beisson, Fred
Peltier, Gilles
Li-Beisson, Yonghua - Abstract:
- Abstract : The degradation of branched-chain amino acids provides carbon precursors for lipid biosynthesis during nitrogen starvation and ATP for lipid remobilization upon nitrogen resupply in green algae. Abstract: Nitrogen (N) starvation-induced triacylglycerol (TAG) synthesis, and its complex relationship with starch metabolism in algal cells, has been intensively studied; however, few studies have examined the interaction between amino acid metabolism and TAG biosynthesis. Here, via a forward genetic screen for TAG homeostasis, we isolated a Chlamydomonas ( Chlamydomonas reinhardtii ) mutant ( bkdE1α ) that is deficient in the E1α subunit of the branched-chain ketoacid dehydrogenase (BCKDH) complex. Metabolomics analysis revealed a defect in the catabolism of branched-chain amino acids in bkdE1α . Furthermore, this mutant accumulated 30% less TAG than the parental strain during N starvation and was compromised in TAG remobilization upon N resupply. Intriguingly, the rate of mitochondrial respiration was 20% to 35% lower in bkdE1α compared with the parental strains. Three additional knockout mutants of the other components of the BCKDH complex exhibited phenotypes similar to that of bkdE1α . Transcriptional responses of BCKDH to different N status were consistent with its role in TAG homeostasis. Collectively, these results indicate that branched-chain amino acid catabolism contributes to TAG metabolism by providing carbon precursors and ATP, thus highlighting the complexAbstract : The degradation of branched-chain amino acids provides carbon precursors for lipid biosynthesis during nitrogen starvation and ATP for lipid remobilization upon nitrogen resupply in green algae. Abstract: Nitrogen (N) starvation-induced triacylglycerol (TAG) synthesis, and its complex relationship with starch metabolism in algal cells, has been intensively studied; however, few studies have examined the interaction between amino acid metabolism and TAG biosynthesis. Here, via a forward genetic screen for TAG homeostasis, we isolated a Chlamydomonas ( Chlamydomonas reinhardtii ) mutant ( bkdE1α ) that is deficient in the E1α subunit of the branched-chain ketoacid dehydrogenase (BCKDH) complex. Metabolomics analysis revealed a defect in the catabolism of branched-chain amino acids in bkdE1α . Furthermore, this mutant accumulated 30% less TAG than the parental strain during N starvation and was compromised in TAG remobilization upon N resupply. Intriguingly, the rate of mitochondrial respiration was 20% to 35% lower in bkdE1α compared with the parental strains. Three additional knockout mutants of the other components of the BCKDH complex exhibited phenotypes similar to that of bkdE1α . Transcriptional responses of BCKDH to different N status were consistent with its role in TAG homeostasis. Collectively, these results indicate that branched-chain amino acid catabolism contributes to TAG metabolism by providing carbon precursors and ATP, thus highlighting the complex interplay between distinct subcellular metabolisms for oil storage in green microalgae. … (more)
- Is Part Of:
- Plant physiology. Volume 179:Issue 4(2019)
- Journal:
- Plant physiology
- Issue:
- Volume 179:Issue 4(2019)
- Issue Display:
- Volume 179, Issue 4 (2019)
- Year:
- 2019
- Volume:
- 179
- Issue:
- 4
- Issue Sort Value:
- 2019-0179-0004-0000
- Page Start:
- 1502
- Page End:
- 1514
- Publication Date:
- 2019-02-06
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1104/pp.18.01584 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 16196.xml