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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1016/j.plantsci.2018.07.011
|2 doi
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|a pubmed24n0958.xml
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|a (DE-627)NLM287467791
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|a (NLM)30107884
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|a (PII)S0168-9452(18)30541-7
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Rosli, Rozana
|e verfasserin
|4 aut
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| 245 |
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|a In silico characterization and expression profiling of the diacylglycerol acyltransferase gene family (DGAT1, DGAT2, DGAT3 and WS/DGAT) from oil palm, Elaeis guineensis
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|c 2018
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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|a Date Completed 15.10.2018
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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 Copyright © 2018 Elsevier B.V. All rights reserved.
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|a The diacylglycerol acyltransferases (DGAT) (diacylglycerol:acyl-CoA acyltransferase, EC 2.3.1.20) are a key group of enzymes that catalyse the final and usually the most important rate-limiting step of triacylglycerol biosynthesis in plants and other organisms. Genes encoding four distinct functional families of DGAT enzymes have been characterised in the genome of the African oil palm, Elaeis guineensis. The contrasting features of the various isoforms within the four families of DGAT genes, namely DGAT1, DGAT2, DGAT3 and WS/DGAT are presented both in the oil palm itself and, for comparative purposes, in 12 other oil crop or model/related plants, namely Arabidopsis thaliana, Brachypodium distachyon, Brassica napus, Elaeis oleifera, Glycine max, Gossypium hirsutum, Helianthus annuus, Musa acuminata, Oryza sativa, Phoenix dactylifera, Sorghum bicolor, and Zea mays. The oil palm genome contains respectively three, two, two and two distinctly expressed functional copies of the DGAT1, DGAT2, DGAT3 and WS/DGAT genes. Phylogenetic analyses of the four DGAT families showed that the E. guineensis genes tend to cluster with sequences from P. dactylifera and M. acuminata rather than with other members of the Commelinid monocots group, such as the Poales which include the major cereal crops such as rice and maize. Comparison of the predicted DGAT protein sequences with other animal and plant DGATs was consistent with the E. guineensis DGAT1 being ER located with its active site facing the lumen while DGAT2, although also ER located, had a predicted cytosol-facing active site. In contrast, DGAT3 and some (but not all) WS/DGAT in E. guineensis are predicted to be soluble, cytosolic enzymes. Evaluation of E. guineensis DGAT gene expression in different tissues and developmental stages suggests that the four DGAT groups have distinctive physiological roles and are particularly prominent in developmental processes relating to reproduction, such as flowering, and in fruit/seed formation especially in the mesocarp and endosperm tissues
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|a Journal Article
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|a Diacylglycerol acyltransferase (DGAT)
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|a Endosperm
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|a Kernel
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|a Mesocarp
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|a Oil palm (Elaeis guineensis)
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|a Triacylglycerol
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| 650 |
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|a Diacylglycerol O-Acyltransferase
|2 NLM
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| 650 |
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|a EC 2.3.1.20
|2 NLM
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| 700 |
1 |
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|a Chan, Pek-Lan
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Chan, Kuang-Lim
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Amiruddin, Nadzirah
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Low, Eng-Ti Leslie
|e verfasserin
|4 aut
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| 700 |
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|a Singh, Rajinder
|e verfasserin
|4 aut
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|a Harwood, John L
|e verfasserin
|4 aut
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| 700 |
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|a Murphy, Denis J
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Plant science : an international journal of experimental plant biology
|d 1985
|g 275(2018) vom: 14. Okt., Seite 84-96
|w (DE-627)NLM098174193
|x 1873-2259
|7 nnns
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| 773 |
1 |
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|g volume:275
|g year:2018
|g day:14
|g month:10
|g pages:84-96
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| 856 |
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|u http://dx.doi.org/10.1016/j.plantsci.2018.07.011
|3 Volltext
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