Identification and biochemical characterization of five long-chain acyl-coenzyme A synthetases from the diatom Phaeodactylum tricornutum

Copyright © 2013 Elsevier Masson SAS. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Plant physiology and biochemistry : PPB. - 1991. - 74(2014) vom: 21. Jan., Seite 33-41
1. Verfasser: Guo, Xiaojing (VerfasserIn)
Weitere Verfasser: Jiang, Mulan, Wan, Xia, Hu, Chuanjiong, Gong, Yangmin
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
Zugriff auf das übergeordnete Werk:Plant physiology and biochemistry : PPB
Schlagworte:Journal Article Research Support, Non-U.S. Gov't 4,4-Difluro-5-methyl-4-bora-3,4-diaza-s-indacene-3-dodecanoic acid ACP ACSL BSA C(1)-BODIPY-C(12) Fatty acids Phaeodactylum tricornutum QRT-PCR mehr... RACE TAG VLCS/FATP Yeast acyl–acyl carrier protein bovine serum albumin long-chain acyl-CoA synthetase quantitative reverse transcription PCR rapid amplification of cDNA end triacylglycerol very long-chain acyl-CoA synthetase/fatty acid transport protein Fatty Acids Coenzyme A Ligases EC 6.2.1.-
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245 1 0 |a Identification and biochemical characterization of five long-chain acyl-coenzyme A synthetases from the diatom Phaeodactylum tricornutum 
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520 |a Long-chain acyl-CoA synthetase (ACSL; EC 6.2.1.3) catalyzes the conversion of free fatty acid to acyl-CoA ester, which is necessary for many pathways of fatty acid and lipid metabolism. The diatom Phaeodactylum tricornutum genome encodes five putative ACSLs (PtACSL1-5) that contain several highly conserved motifs and share limited sequence similarities with each other and with other known ACSLs. To verify their long-chain acyl-CoA synthetase activities, five cDNAs encoding these PtACSLs were cloned, expressed, and tested for their ability to complement the Saccharomyces cerevisiae double mutant FAA1ΔFAA4Δ. Only two of five PtACSLs were able to restore growth, facilitate exogenous fatty acid uptake, and enhance storage lipid accumulation. We also found that P. tricornutum cells are capable of importing long-chain fatty acids from extracellular environment. The identification of P. tricornutum ACSLs will provide molecular basis for the study of ACSL-mediated lipid synthesis and metabolism in diatoms 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 4 |a 4,4-Difluro-5-methyl-4-bora-3,4-diaza-s-indacene-3-dodecanoic acid 
650 4 |a ACP 
650 4 |a ACSL 
650 4 |a BSA 
650 4 |a C(1)-BODIPY-C(12) 
650 4 |a Fatty acids 
650 4 |a Phaeodactylum tricornutum 
650 4 |a QRT-PCR 
650 4 |a RACE 
650 4 |a TAG 
650 4 |a VLCS/FATP 
650 4 |a Yeast 
650 4 |a acyl–acyl carrier protein 
650 4 |a bovine serum albumin 
650 4 |a long-chain acyl-CoA synthetase 
650 4 |a quantitative reverse transcription PCR 
650 4 |a rapid amplification of cDNA end 
650 4 |a triacylglycerol 
650 4 |a very long-chain acyl-CoA synthetase/fatty acid transport protein 
650 7 |a Fatty Acids  |2 NLM 
650 7 |a Coenzyme A Ligases  |2 NLM 
650 7 |a EC 6.2.1.-  |2 NLM 
700 1 |a Jiang, Mulan  |e verfasserin  |4 aut 
700 1 |a Wan, Xia  |e verfasserin  |4 aut 
700 1 |a Hu, Chuanjiong  |e verfasserin  |4 aut 
700 1 |a Gong, Yangmin  |e verfasserin  |4 aut 
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773 1 8 |g volume:74  |g year:2014  |g day:21  |g month:01  |g pages:33-41 
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