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Article: Roles of multiple acyl-CoA oxidases in the routing of carbon flow towards β-oxidation and polyhydroxyalkanoate biosynthesis in Yarrowia lipolytica

Haddouche, Ramdane / Delessert, Syndie / Sabirova, Julia / Neuvéglise, Cécile / Poirier, Yves / Nicaud, Jean-Marc

FEMS yeast research. 2010 Nov., v. 10, no. 7

2010

Abstract: The oleaginous yeast Yarrowia lipolytica possesses six acyl-CoA oxidase (Aox) isoenzymes encoded by genes POX1-POX6. The respective roles of these multiple Aox isoenzymes were studied in recombinant Y. lipolytica strains that express heterologous ... ...

Abstract	The oleaginous yeast Yarrowia lipolytica possesses six acyl-CoA oxidase (Aox) isoenzymes encoded by genes POX1-POX6. The respective roles of these multiple Aox isoenzymes were studied in recombinant Y. lipolytica strains that express heterologous polyhydroxyalkanoate (PHA) synthase (phaC) of Pseudomonas aeruginosa in varying POX genetic backgrounds, thus allowing assessment of the impact of specific Aox enzymes on the routing of carbon flow to β-oxidation or to PHA biosynthesis. Analysis of PHA production yields during growth on fatty acids with different chain lengths has revealed that the POX genotype significantly affects the PHA levels, but not the monomer composition of PHA. Aox3p function was found to be responsible for 90% and 75% of the total PHA produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of PHA from C9:0 fatty acid. Other Aoxs, such as Aox1p, Aox2p, Aox4p and Aox6p, were not found to play a significant role in PHA biosynthesis, independent of the chain length of the fatty acid used. Finally, three known models of β-oxidation are discussed and it is shown that a 'leaky-hose pipe model' of the cycle can be applied to Y. lipolytica.
Keywords	yeasts ; Yarrowia lipolytica
Language	English
Dates of publication	2010-11
Size	p. 917-927.
Publisher	Blackwell Publishing Ltd
Publishing place	Oxford, UK
Document type	Article
ZDB-ID	2036775-2
ISSN	1567-1364 ; 1567-1356
ISSN (online)	1567-1364
ISSN	1567-1356
DOI	10.1111/j.1567-1364.2010.00670.x
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Article ; Online: Contributions of the peroxisome and β-oxidation cycle to biotin synthesis in fungi.

Magliano, Pasqualina / Flipphi, Michel / Arpat, Bulak A / Delessert, Syndie / Poirier, Yves

The Journal of biological chemistry

2011 Volume 286, Issue 49, Page(s) 42133–42140

Abstract: The first step in the synthesis of the bicyclic rings of D-biotin is mediated by 8-amino-7-oxononanoate (AON) synthase, which catalyzes the decarboxylative condensation of l-alanine and pimelate thioester. We found that the Aspergillus nidulans AON ... ...

Abstract	The first step in the synthesis of the bicyclic rings of D-biotin is mediated by 8-amino-7-oxononanoate (AON) synthase, which catalyzes the decarboxylative condensation of l-alanine and pimelate thioester. We found that the Aspergillus nidulans AON synthase, encoded by the bioF gene, is a peroxisomal enzyme with a type 1 peroxisomal targeting sequence (PTS1). Localization of AON to the peroxisome was essential for biotin synthesis because expression of a cytosolic AON variant or deletion of pexE, encoding the PTS1 receptor, rendered A. nidulans a biotin auxotroph. AON synthases with PTS1 are found throughout the fungal kingdom, in ascomycetes, basidiomycetes, and members of basal fungal lineages but not in representatives of the Saccharomyces species complex, including Saccharomyces cerevisiae. A. nidulans mutants defective in the peroxisomal acyl-CoA oxidase AoxA or the multifunctional protein FoxA showed a strong decrease in colonial growth rate in biotin-deficient medium, whereas partial growth recovery occurred with pimelic acid supplementation. These results indicate that pimeloyl-CoA is the in vivo substrate of AON synthase and that it is generated in the peroxisome via the β-oxidation cycle in A. nidulans and probably in a broad range of fungi. However, the β-oxidation cycle is not essential for biotin synthesis in S. cerevisiae or Escherichia coli. These results suggest that alternative pathways for synthesis of the pimelate intermediate exist in bacteria and eukaryotes and that Saccharomyces species use a pathway different from that used by the majority of fungi.
MeSH term(s)	Acyl Coenzyme A/chemistry ; Aspergillus nidulans/genetics ; Biotin/chemistry ; Escherichia coli/metabolism ; Gene Deletion ; Gene Expression Regulation, Fungal ; Genetic Complementation Test ; Mutation ; Oxidation-Reduction ; Oxygen/chemistry ; Peroxisomes/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism
Chemical Substances	Acyl Coenzyme A ; pimeloyl-coenzyme A (18907-20-5) ; Biotin (6SO6U10H04) ; Oxygen (S88TT14065)
Language	English
Publishing date	2011-10-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.279687
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Article: Analysis of the beta-oxidation of trans-unsaturated fatty acid in recombinant Saccharomyces cerevisiae expressing a peroxisomal PHA synthase reveals the involvement of a reductase-dependent pathway.

Robert, Julien / Marchesini, Silvia / Delessert, Syndie / Poirier, Yves

Biochimica et biophysica acta

2005 Volume 1734, Issue 2, Page(s) 169–177

Abstract: The degradation of fatty acids having cis- or trans-unsaturated bond at an even carbon was analyzed in Saccharomyces cerevisiae by monitoring polyhydroxyalkanoate production in the peroxisome. Polyhydroxyalkanaote is synthesized by the polymerization of ... ...

Abstract	The degradation of fatty acids having cis- or trans-unsaturated bond at an even carbon was analyzed in Saccharomyces cerevisiae by monitoring polyhydroxyalkanoate production in the peroxisome. Polyhydroxyalkanaote is synthesized by the polymerization of the beta-oxidation intermediates 3-hydroxy-acyl-CoAs via a bacterial polyhydroxyalkanoate synthase targeted to the peroxisome. The synthesis of polyhydroxyalkanoate in cells grown in media containing 10-cis-heptadecenoic acid was dependent on the presence of 2,4-dienoyl-CoA reductase activity as well as on Delta3,Delta2-enoyl-CoA isomerase activity. The synthesis of polyhydroxyalkanoate from 10-trans-heptadecenoic acid in mutants devoid of 2,4-dienoyl-CoA reductase revealed degradation of the trans fatty acid directly via the enoyl-CoA hydratase II activity of the multifunctional enzyme (MFE), although the level of polyhydroxyalkanoate was 10-25% to that of wild type cells. Polyhydroxyalkanoate produced from 10-trans-heptadecenoic acid in wild type cells showed substantial carbon flux through both a reductase-dependent and a direct MFE-dependent pathway. Flux through beta-oxidation was more severely reduced in mutants devoid of Delta3,Delta2-enoyl-CoA isomerase compared to mutants devoid of 2,4-dienoyl-CoA reductase. It is concluded that the intermediate 2-trans,4-trans-dienoyl-CoA is metabolized in vivo in yeast by both the enoyl-CoA hydratase II activity of the multifunctional protein and the 2,4-dienoyl-CoA reductase, and that the synthesis of the intermediate 3-trans-enoyl-CoA in the absence of the Delta3,Delta2-enoyl-CoA isomerase leads to the blockage of the direct MFE-dependent pathway in vivo.
MeSH term(s)	Acyltransferases/genetics ; Acyltransferases/metabolism ; Culture Media/chemistry ; Fatty Acids, Unsaturated/chemistry ; Molecular Conformation ; Oxidation-Reduction ; Oxidoreductases/metabolism ; Peroxisomes/chemistry ; Peroxisomes/enzymology ; Pseudomonas aeruginosa/enzymology ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics
Chemical Substances	Culture Media ; Fatty Acids, Unsaturated ; Oxidoreductases (EC 1.-) ; Acyltransferases (EC 2.3.-) ; poly(3-hydroxyalkanoic acid) synthase (EC 2.3.1.-)
Language	English
Publishing date	2005-05-15
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbalip.2005.02.010
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Article: Analysis of the contribution of the beta-oxidation auxiliary enzymes in the degradation of the dietary conjugated linoleic acid 9-cis-11-trans-octadecadienoic acid in the peroxisomes of Saccharomyces cerevisiae.

Bogdawa, Heique / Delessert, Syndie / Poirier, Yves

Biochimica et biophysica acta

2005 Volume 1735, Issue 3, Page(s) 204–213

Abstract: Beta-oxidation of the conjugated linoleic acid 9-cis,11-trans-octadecadienoic acid (rumenic acid) was analyzed in vivo in Saccharomyces cerevisiae by monitoring polyhydroxyalkanoate production in the peroxisome. Polyhydroxyalkanoate is synthesized by the ...

Abstract	Beta-oxidation of the conjugated linoleic acid 9-cis,11-trans-octadecadienoic acid (rumenic acid) was analyzed in vivo in Saccharomyces cerevisiae by monitoring polyhydroxyalkanoate production in the peroxisome. Polyhydroxyalkanoate is synthesized by the polymerization of the beta-oxidation intermediates 3-hydroxyacyl-CoAs via a bacterial polyhydroxyalkanoate synthase targeted to the peroxisome. The amount of polyhydroxyalkanaote synthesized from the degradation of rumenic acid was found to be similar to the amount synthesized from the degradation of 10-trans,12-cis-octadecadienoic acid, oleic acid or 10-cis-heptadecenoic acid. Furthermore, the degradation of 10-cis-heptadecenoic acid was found to be unaffected by the presence of rumenic acid in the media. Efficient degradation of rumenic acid was found to be independent of the Delta(3,5),Delta(2,4)-dienoyl-CoA isomerase but instead relied on the presence of Delta(3),Delta(2)-enoyl-CoA isomerase activity. The presence of the unsaturated monomer 3-hydroxydodecenoic acid in polyhydroxyalkanoate derived from rumenic acid degradation was found to be dependent on the presence of a Delta(3),Delta(2)-enoyl-CoA isomerase activity. Together, these data indicate that rumenic acid is mainly degraded in vivo in S. cerevisiae through a pathway requiring only the participation of the auxiliary enzymes Delta(3),Delta(2)-enoyl-CoA isomerase, along with the enzyme of the core beta-oxidation cycle.
MeSH term(s)	Linoleic Acids/metabolism ; Linoleic Acids, Conjugated/metabolism ; Oxidation-Reduction ; Peroxisomes/enzymology ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Linoleic Acids ; Linoleic Acids, Conjugated ; Saccharomyces cerevisiae Proteins ; 9,11-linoleic acid (1839-11-8) ; octadeca-5,8-dienoic acid (2197-50-4)
Language	English
Publishing date	2005-08-15
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbalip.2005.06.003
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Article: Level of accumulation of epoxy fatty acid in Arabidopsis thaliana expressing a linoleic acid delta12-epoxygenase is influenced by the availability of the substrate linoleic acid.

Rezzonico, Enea / Moire, Laurence / Delessert, Syndie / Poirier, Yves

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

2004 Volume 109, Issue 5, Page(s) 1077–1082

Abstract: Arabidopsis thaliana (L.) Heynh. expressing the Crepis palaestina (L.) linoleic acid delta12-epoxygenase in its developing seeds typically accumulates low levels of vernolic acid (12,13-epoxy-octadec-cis-9-enoic acid) in comparison to levels found in ... ...

Abstract	Arabidopsis thaliana (L.) Heynh. expressing the Crepis palaestina (L.) linoleic acid delta12-epoxygenase in its developing seeds typically accumulates low levels of vernolic acid (12,13-epoxy-octadec-cis-9-enoic acid) in comparison to levels found in seeds of the native C. palaestina. In order to determine some of the factors limiting the accumulation of this unusual fatty acid, we have examined the effects of increasing the availability of linoleic acid (9cis, 12cis-octadecadienoic acid), the substrate of the delta12-epoxygenase, on the quantity of epoxy fatty acids accumulating in transgenic A. thaliana. The addition of linoleic acid to liquid cultures of transgenic plants expressing the delta12-epoxygenase under the control of the cauliflower mosaic virus 35S promoter increased the amount of vernolic acid in vegetative tissues by 2.8-fold. In contrast, the addition to these cultures of linoelaidic acid (9trans, 12trans-octadecadienoic acid), which is not a substrate of the delta12-epoxygenase, resulted in a slight decrease in vernolic acid accumulation. Expression of the delta12-epoxygenase under the control of the napin promoter in the A. thaliana triple mutant fad3/fad7-1/fad9, which is deficient in the synthesis of tri-unsaturated fatty acids and has a 60% higher level of linoleic acid than the wild type, was found to increase the average vernolic acid content of the seeds by 55% compared to the expression of the delta12-epoxygenase in a wild-type background. Together, these results reveal that the availability of linoleic acid is an important factor affecting the synthesis of epoxy fatty acid in transgenic plants.
MeSH term(s)	Arabidopsis/genetics ; Arabidopsis/metabolism ; Caulimovirus/genetics ; Epoxy Compounds ; Gene Transfer Techniques ; Linoleic Acid/metabolism ; Oleic Acids/biosynthesis ; Oxidoreductases/genetics ; Oxidoreductases/metabolism ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Plants, Genetically Modified/genetics ; Plants, Genetically Modified/metabolism ; Promoter Regions, Genetic/genetics ; Seeds/metabolism
Chemical Substances	Epoxy Compounds ; Oleic Acids ; Plant Proteins ; vernolic acid (503-07-1) ; Linoleic Acid (9KJL21T0QJ) ; Oxidoreductases (EC 1.-) ; epoxygenase, Crepis palaestina (EC 1.-)
Language	English
Publishing date	2004-09
Publishing country	Germany
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2170-2
ISSN	1432-2242 ; 0040-5752
ISSN (online)	1432-2242
ISSN	0040-5752
DOI	10.1007/s00122-004-1721-x
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Article: Engineering polyhydroxyalkanoate content and monomer composition in the oleaginous yeast Yarrowia lipolytica by modifying the ß-oxidation multifunctional protein

Haddouche, Ramdane / Poirier, Yves / Delessert, Syndie / Sabirova, Julia / Pagot, Yves / Neuvéglise, Cécile / Nicaud, Jean-Marc

Applied microbiology and biotechnology.. 2011 Sept., v. 91, no. 5

2011

Abstract: Recombinant strains of the oleaginous yeast Yarrowia lipolytica expressing the PHA synthase gene (PhaC) from Pseudomonas aeruginosa in the peroxisome were found able to produce polyhydroxyalkanoates (PHA). PHA production yield, but not the monomer ... ...

Abstract	Recombinant strains of the oleaginous yeast Yarrowia lipolytica expressing the PHA synthase gene (PhaC) from Pseudomonas aeruginosa in the peroxisome were found able to produce polyhydroxyalkanoates (PHA). PHA production yield, but not the monomer composition, was dependent on POX genotype (POX genes encoding acyl-CoA oxidases) (Haddouche et al. FEMS Yeast Res 10:917–927, 2010). In this study of variants of the Y. lipolytica β-oxidation multifunctional enzyme, with deletions or inactivations of the R-3-hydroxyacyl-CoA dehydrogenase domain, we were able to produce hetero-polymers (functional MFE enzyme) or homo-polymers (with no 3-hydroxyacyl-CoA dehydrogenase activity) of PHA consisting principally of 3-hydroxyacid monomers (>80%) of the same length as the external fatty acid used for growth. The redirection of fatty acid flux towards β-oxidation, by deletion of the neutral lipid synthesis pathway (mutant strain Q4 devoid of the acyltransferases encoded by the LRO1, DGA1, DGA2 and ARE1 genes), in combination with variant expressing only the enoyl-CoA hydratase 2 domain, led to a significant increase in PHA levels, to 7.3% of cell dry weight. Finally, the presence of shorter monomers (up to 20% of the monomers) in a mutant strain lacking the peroxisomal 3-hydroxyacyl-CoA dehydrogenase domain provided evidence for the occurrence of partial mitochondrial β-oxidation in Y. lipolytica.
Keywords	Pseudomonas aeruginosa ; Yarrowia lipolytica ; acyl coenzyme A ; acyltransferases ; fatty acids ; genes ; genotype ; proteins ; triacylglycerols ; yeasts
Language	English
Dates of publication	2011-09
Size	p. 1327-1340.
Publishing place	Springer-Verlag
Document type	Article
ZDB-ID	392453-1
ISSN	1432-0614 ; 0171-1741 ; 0175-7598
ISSN (online)	1432-0614
ISSN	0171-1741 ; 0175-7598
DOI	10.1007/s00253-011-3331-2
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Article ; Online: Roles of multiple acyl-CoA oxidases in the routing of carbon flow towards β-oxidation and polyhydroxyalkanoate biosynthesis in Yarrowia lipolytica.

Haddouche, Ramdane / Delessert, Syndie / Sabirova, Julia / Neuvéglise, Cécile / Poirier, Yves / Nicaud, Jean-Marc

FEMS yeast research

2010 Volume 10, Issue 7, Page(s) 917–927

Abstract	The oleaginous yeast Yarrowia lipolytica possesses six acyl-CoA oxidase (Aox) isoenzymes encoded by genes POX1-POX6. The respective roles of these multiple Aox isoenzymes were studied in recombinant Y. lipolytica strains that express heterologous polyhydroxyalkanoate (PHA) synthase (phaC) of Pseudomonas aeruginosa in varying POX genetic backgrounds, thus allowing assessment of the impact of specific Aox enzymes on the routing of carbon flow to β-oxidation or to PHA biosynthesis. Analysis of PHA production yields during growth on fatty acids with different chain lengths has revealed that the POX genotype significantly affects the PHA levels, but not the monomer composition of PHA. Aox3p function was found to be responsible for 90% and 75% of the total PHA produced from either C9:0 or C13:0 fatty acid, respectively, whereas Aox5p encodes the main Aox involved in the biosynthesis of 70% of PHA from C9:0 fatty acid. Other Aoxs, such as Aox1p, Aox2p, Aox4p and Aox6p, were not found to play a significant role in PHA biosynthesis, independent of the chain length of the fatty acid used. Finally, three known models of β-oxidation are discussed and it is shown that a 'leaky-hose pipe model' of the cycle can be applied to Y. lipolytica.
MeSH term(s)	Acyl-CoA Oxidase/metabolism ; Acyltransferases/genetics ; Acyltransferases/metabolism ; Carbon/metabolism ; Fatty Acids/metabolism ; Oxidation-Reduction ; Polyhydroxyalkanoates/metabolism ; Pseudomonas aeruginosa/enzymology ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Yarrowia/enzymology ; Yarrowia/growth & development ; Yarrowia/metabolism
Chemical Substances	Fatty Acids ; Polyhydroxyalkanoates ; Recombinant Proteins ; Carbon (7440-44-0) ; Acyl-CoA Oxidase (EC 1.3.3.6) ; Acyltransferases (EC 2.3.-) ; poly(3-hydroxyalkanoic acid) synthase (EC 2.3.1.-)
Language	English
Publishing date	2010-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2036775-2
ISSN	1567-1364 ; 1567-1356
ISSN (online)	1567-1364
ISSN	1567-1356
DOI	10.1111/j.1567-1364.2010.00670.x
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Article: Peroxisomal Δ³,Δ²-enoyl CoA isomerases and evolution of cytosolic paralogues in embryophytes

Goepfert, Simon / Vidoudez, Charles / Tellgren-Roth, Christian / Delessert, Syndie / Hiltunen, J. Kalervo / Poirier, Yves

Plant journal. 2008 Dec., v. 56, no. 5

2008

Abstract: Δ³,Δ²-enoyl CoA isomerase (ECI) is an enzyme that participates in the degradation of unsaturated fatty acids through the β-oxidation cycle. Three genes encoding Δ³,Δ²-enoyl CoA isomerases and named AtECI1, AtECI2 and AtECI3 have been identified in ... ...

Abstract	Δ³,Δ²-enoyl CoA isomerase (ECI) is an enzyme that participates in the degradation of unsaturated fatty acids through the β-oxidation cycle. Three genes encoding Δ³,Δ²-enoyl CoA isomerases and named AtECI1, AtECI2 and AtECI3 have been identified in Arabidopsis thaliana. When expressed heterologously in Saccharomyces cerevisiae, all three ECI proteins were targeted to the peroxisomes and enabled the yeast Δeci1 mutant to degrade 10Z-heptadecenoic acid, demonstrating Δ³,Δ²-enoyl CoA isomerase activity in vivo. Fusion proteins between yellow fluorescent protein and AtECI1 or AtECI2 were targeted to the peroxisomes in onion epidermal cells and Arabidopsis root cells, but a similar fusion protein with AtECI3 remained in the cytosol for both tissues. AtECI3 targeting to peroxisomes in S. cerevisiae was dependent on yeast PEX5, while expression of Arabidopsis PEX5 in yeast failed to target AtECI3 to peroxisomes. AtECI2 and AtECI3 are tandem duplicated genes and show a high level of amino acid conservation, except at the C-terminus; AtECI2 ends with the well conserved peroxisome targeting signal 1 (PTS1) terminal tripeptide PKL, while AtECI3 possesses a divergent HNL terminal tripeptide. Evolutionary analysis of ECI genes in plants revealed several independent duplication events, with duplications occurring in rice and Medicago truncatula, generating homologues with divergent C-termini and no recognizable PTS1. All plant ECI genes analyzed, including AtECI3, are under negative purifying selection, implying functionality of the cytosolic AtECI3. Analysis of the mammalian and fungal genomes failed to identify cytosolic variants of the Δ³,Δ²-enoyl CoA isomerase, indicating that evolution of cytosolic Δ³,Δ²-enoyl CoA isomerases is restricted to the plant kingdom.
Keywords	Arabidopsis
Language	English
Dates of publication	2008-12
Size	p. 728-742.
Publisher	Blackwell Publishing Ltd
Publishing place	Oxford, UK
Document type	Article
ZDB-ID	1088037-9
ISSN	1365-313X ; 0960-7412
ISSN (online)	1365-313X
ISSN	0960-7412
DOI	10.1111/j.1365-313X.2008.03635.x
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Article ; Online: Peroxisomal Delta(3),Delta(2)-enoyl CoA isomerases and evolution of cytosolic paralogues in embryophytes.

Goepfert, Simon / Vidoudez, Charles / Tellgren-Roth, Christian / Delessert, Syndie / Hiltunen, J Kalervo / Poirier, Yves

The Plant journal : for cell and molecular biology

2008 Volume 56, Issue 5, Page(s) 728–742

Abstract: Delta(3),Delta(2)-enoyl CoA isomerase (ECI) is an enzyme that participates in the degradation of unsaturated fatty acids through the beta-oxidation cycle. Three genes encoding Delta(3),Delta(2)-enoyl CoA isomerases and named AtECI1, AtECI2 and AtECI3 ... ...

Abstract	Delta(3),Delta(2)-enoyl CoA isomerase (ECI) is an enzyme that participates in the degradation of unsaturated fatty acids through the beta-oxidation cycle. Three genes encoding Delta(3),Delta(2)-enoyl CoA isomerases and named AtECI1, AtECI2 and AtECI3 have been identified in Arabidopsis thaliana. When expressed heterologously in Saccharomyces cerevisiae, all three ECI proteins were targeted to the peroxisomes and enabled the yeast Deltaeci1 mutant to degrade 10Z-heptadecenoic acid, demonstrating Delta(3),Delta(2)-enoyl CoA isomerase activity in vivo. Fusion proteins between yellow fluorescent protein and AtECI1 or AtECI2 were targeted to the peroxisomes in onion epidermal cells and Arabidopsis root cells, but a similar fusion protein with AtECI3 remained in the cytosol for both tissues. AtECI3 targeting to peroxisomes in S. cerevisiae was dependent on yeast PEX5, while expression of Arabidopsis PEX5 in yeast failed to target AtECI3 to peroxisomes. AtECI2 and AtECI3 are tandem duplicated genes and show a high level of amino acid conservation, except at the C-terminus; AtECI2 ends with the well conserved peroxisome targeting signal 1 (PTS1) terminal tripeptide PKL, while AtECI3 possesses a divergent HNL terminal tripeptide. Evolutionary analysis of ECI genes in plants revealed several independent duplication events, with duplications occurring in rice and Medicago truncatula, generating homologues with divergent C-termini and no recognizable PTS1. All plant ECI genes analyzed, including AtECI3, are under negative purifying selection, implying functionality of the cytosolic AtECI3. Analysis of the mammalian and fungal genomes failed to identify cytosolic variants of the Delta(3),Delta(2)-enoyl CoA isomerase, indicating that evolution of cytosolic Delta(3),Delta(2)-enoyl CoA isomerases is restricted to the plant kingdom.
MeSH term(s)	Amino Acid Sequence ; Arabidopsis/enzymology ; Arabidopsis/genetics ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Carbon-Carbon Double Bond Isomerases/genetics ; Carbon-Carbon Double Bond Isomerases/metabolism ; Cytosol/enzymology ; Dodecenoyl-CoA Isomerase ; Evolution, Molecular ; Fatty Acids, Unsaturated/metabolism ; Gene Duplication ; Gene Expression Profiling ; Genes, Plant ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Molecular Sequence Data ; Peroxisome-Targeting Signal 1 Receptor ; Peroxisomes/enzymology ; Phylogeny ; RNA, Plant/genetics ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae/genetics ; Selection, Genetic ; Sequence Alignment ; Sequence Analysis, DNA
Chemical Substances	Arabidopsis Proteins ; Fatty Acids, Unsaturated ; Luminescent Proteins ; Peroxisome-Targeting Signal 1 Receptor ; RNA, Plant ; Receptors, Cytoplasmic and Nuclear ; Recombinant Proteins ; Carbon-Carbon Double Bond Isomerases (EC 5.3.3.-) ; Dodecenoyl-CoA Isomerase (EC 5.3.3.8)
Language	English
Publishing date	2008-12
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1088037-9
ISSN	1365-313X ; 0960-7412
ISSN (online)	1365-313X
ISSN	0960-7412
DOI	10.1111/j.1365-313X.2008.03635.x
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Article: The Peroxisomal Acyl-CoA Thioesterase Pte1p from Saccharomyces cerevisiae Is Required for Efficient Degradation of Short Straight Chain and Branched Chain Fatty Acids

Maeda, Isamu / Delessert, Syndie / Hasegawa, Seiko / Seto, Yoshiaki / Zuber, Sophie / Poirier, Yves

Journal of biological chemistry. 2006 Apr. 28, v. 281, no. 17

2006

Abstract: The role of the Saccharomyces cerevisae peroxisomal acyl-coenzyme A (acyl-CoA) thioesterase (Pte1p) in fatty acid [beta]-oxidation was studied by analyzing the in vitro kinetic activity of the purified protein as well as by measuring the carbon flux ... ...

Abstract	The role of the Saccharomyces cerevisae peroxisomal acyl-coenzyme A (acyl-CoA) thioesterase (Pte1p) in fatty acid [beta]-oxidation was studied by analyzing the in vitro kinetic activity of the purified protein as well as by measuring the carbon flux through the [beta]-oxidation cycle in vivo using the synthesis of peroxisomal polyhydroxyalkanoate (PHA) from the polymerization of the 3-hydroxyacyl-CoAs as a marker. The amount of PHA synthesized from the degradation of 10-cis-heptadecenoic, tridecanoic, undecanoic, or nonanoic acids was equivalent or slightly reduced in the pte1[Delta] strain compared with wild type. In contrast, a strong reduction in PHA synthesized from heptanoic acid and 8-methyl-nonanoic acid was observed for the pte1[Delta] strain compared with wild type. The poor catabolism of 8-methyl-nonanoic acid via [beta]-oxidation in pte1[Delta] negatively impacted the degradation of 10-cis-heptadecenoic acid and reduced the ability of the cells to efficiently grow in medium containing such fatty acids. An increase in the proportion of the short chain 3-hydroxyacid monomers was observed in PHA synthesized in pte1[Delta] cells grown on a variety of fatty acids, indicating a reduction in the metabolism of short chain acyl-CoAs in these cells. A purified histidine-tagged Pte1p showed high activity toward short and medium chain length acyl-CoAs, including butyryl-CoA, decanoyl-CoA and 8-methyl-nonanoyl-CoA. The kinetic parameters measured for the purified Pte1p fit well with the implication of this enzyme in the efficient metabolism of short straight and branched chain fatty acyl-CoAs by the [beta]-oxidation cycle.
Language	English
Dates of publication	2006-0428
Size	p. 11729-11735.
Publishing place	American Society for Biochemistry and Molecular Biology
Document type	Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
Database	NAL-Catalogue (AGRICOLA)

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