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231225s2019 xx |||||o 00| ||eng c |
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|a 10.1111/nph.16000
|2 doi
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|a pubmed25n0994.xml
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|a (DE-627)NLM298281252
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|a (NLM)31211859
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Angkawijaya, Artik Elisa
|e verfasserin
|4 aut
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| 245 |
1 |
0 |
|a LYSOPHOSPHATIDIC ACID ACYLTRANSFERASES 4 and 5 are involved in glycerolipid metabolism and nitrogen starvation response in Arabidopsis
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|c 2019
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 04.05.2020
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2019 The Authors. New Phytologist © 2019 New Phytologist Trust.
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|a Nitrogen (N) deficiency triggers an accumulation of a storage lipid triacylglycerol (TAG) in seed plants and algae. Whereas the metabolic pathway and regulatory mechanism to synthesize TAG from diacylglycerol are well known, enzymes involved in the supply of diacylglycerol remain elusive under N starvation. Lysophosphatidic acid acyltransferase (LPAT) catalyzes an important step of the de novo phospholipid biosynthesis pathway and thus has a strong flux control in the biosynthesis of phospholipids and TAG. Five LPAT isoforms are known in Arabidopsis; however, the functions of LPAT4 and LPAT5 remain elusive. Here, we show that LPAT4 and LPAT5 are functional endoplasmic-reticulum-localized LPATs. Seedlings of the double knockout mutant lpat4-1 lpat5-1 showed reduced content of phospholipids and TAG under normal growth condition. Under N starvation, lpat4-1 lpat5-1 seedlings showed severer growth defect than the wild-type in shoot. The phenotype was similar to dgat1-4, which affects a major TAG biosynthesis pathway and showed similarly reduced TAG content as the lpat4-1 lpat5-1. We suggest that LPAT4 and LPAT5 may redundantly function in endoplasmic-reticulum-localized de novo glycerolipid biosynthesis for phospholipids and TAG, which is important for the N starvation response in Arabidopsis
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Arabidopsis thaliana
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|a lysophosphatidic acid acyltransferase
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| 650 |
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|a nitrogen starvation
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|a phospholipid biosynthesis
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|a triacylglycerol
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| 650 |
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|a Arabidopsis Proteins
|2 NLM
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|a DNA, Bacterial
|2 NLM
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| 650 |
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|a Fatty Acids
|2 NLM
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| 650 |
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|a Phosphatidic Acids
|2 NLM
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| 650 |
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|a Recombinant Proteins
|2 NLM
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| 650 |
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|a T-DNA
|2 NLM
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| 650 |
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|a Triglycerides
|2 NLM
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| 650 |
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|a 1-Acylglycerol-3-Phosphate O-Acyltransferase
|2 NLM
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| 650 |
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7 |
|a EC 2.3.1.51
|2 NLM
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| 650 |
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|a At1g75020 protein, Arabidopsis
|2 NLM
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| 650 |
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|a EC 2.3.1.51
|2 NLM
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| 650 |
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7 |
|a At3g18850 protein, Arabidopsis
|2 NLM
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| 650 |
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|a EC 2.3.1.51
|2 NLM
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| 650 |
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|a Nitrogen
|2 NLM
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| 650 |
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|a N762921K75
|2 NLM
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| 700 |
1 |
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|a Nguyen, Van Cam
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Nakamura, Yuki
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t The New phytologist
|d 1984
|g 224(2019), 1 vom: 10. Okt., Seite 336-351
|w (DE-627)NLM09818248X
|x 1469-8137
|7 nnns
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| 773 |
1 |
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|g volume:224
|g year:2019
|g number:1
|g day:10
|g month:10
|g pages:336-351
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| 856 |
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|u http://dx.doi.org/10.1111/nph.16000
|3 Volltext
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|a GBV_ILN_350
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|a AR
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|d 224
|j 2019
|e 1
|b 10
|c 10
|h 336-351
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