Engineering polyhydroxyalkanoate content and monomer composition in the oleaginous yeast Yarrowia lipolytica by modifying the ß-oxidation multifunctional protein.
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| Title: | Engineering polyhydroxyalkanoate content and monomer composition in the oleaginous yeast Yarrowia lipolytica by modifying the ß-oxidation multifunctional protein. |
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| Authors: | Haddouche, Ramdane1, Poirier, Yves2, Delessert, Syndie2, Sabirova, Julia1,3, Pagot, Yves1, Neuvéglise, Cécile1, Nicaud, Jean-Marc4,5 jean-marc.nicaud@grignon.inra.fr |
| Source: | Applied Microbiology & Biotechnology. Sep2011, Vol. 91 Issue 5, p1327-1340. 14p. |
| Subjects: | Yeast research, Poly-beta-hydroxyalkanoates, Peroxisomes, Monomers, Pseudomonas aeruginosa, Fatty acids, Molecular genetics, Macromolecules |
| 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, ). 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. [ABSTRACT FROM AUTHOR] |
| Copyright of Applied Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
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| Header | DbId: egs DbLabel: Engineering Source An: 63994783 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Engineering polyhydroxyalkanoate content and monomer composition in the oleaginous yeast Yarrowia lipolytica by modifying the ß-oxidation multifunctional protein. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Haddouche%2C+Ramdane%22">Haddouche, Ramdane</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Poirier%2C+Yves%22">Poirier, Yves</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Delessert%2C+Syndie%22">Delessert, Syndie</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Sabirova%2C+Julia%22">Sabirova, Julia</searchLink><relatesTo>1,3</relatesTo><br /><searchLink fieldCode="AR" term="%22Pagot%2C+Yves%22">Pagot, Yves</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Neuvéglise%2C+Cécile%22">Neuvéglise, Cécile</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Nicaud%2C+Jean-Marc%22">Nicaud, Jean-Marc</searchLink><relatesTo>4,5</relatesTo><i> jean-marc.nicaud@grignon.inra.fr</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Applied+Microbiology+%26+Biotechnology%22">Applied Microbiology & Biotechnology</searchLink>. Sep2011, Vol. 91 Issue 5, p1327-1340. 14p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Yeast+research%22">Yeast research</searchLink><br /><searchLink fieldCode="DE" term="%22Poly-beta-hydroxyalkanoates%22">Poly-beta-hydroxyalkanoates</searchLink><br /><searchLink fieldCode="DE" term="%22Peroxisomes%22">Peroxisomes</searchLink><br /><searchLink fieldCode="DE" term="%22Monomers%22">Monomers</searchLink><br /><searchLink fieldCode="DE" term="%22Pseudomonas+aeruginosa%22">Pseudomonas aeruginosa</searchLink><br /><searchLink fieldCode="DE" term="%22Fatty+acids%22">Fatty acids</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+genetics%22">Molecular genetics</searchLink><br /><searchLink fieldCode="DE" term="%22Macromolecules%22">Macromolecules</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: 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, ). 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. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Applied Microbiology & Biotechnology is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1007/s00253-011-3331-2 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 14 StartPage: 1327 Subjects: – SubjectFull: Yeast research Type: general – SubjectFull: Poly-beta-hydroxyalkanoates Type: general – SubjectFull: Peroxisomes Type: general – SubjectFull: Monomers Type: general – SubjectFull: Pseudomonas aeruginosa Type: general – SubjectFull: Fatty acids Type: general – SubjectFull: Molecular genetics Type: general – SubjectFull: Macromolecules Type: general Titles: – TitleFull: Engineering polyhydroxyalkanoate content and monomer composition in the oleaginous yeast Yarrowia lipolytica by modifying the ß-oxidation multifunctional protein. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Haddouche, Ramdane – PersonEntity: Name: NameFull: Poirier, Yves – PersonEntity: Name: NameFull: Delessert, Syndie – PersonEntity: Name: NameFull: Sabirova, Julia – PersonEntity: Name: NameFull: Pagot, Yves – PersonEntity: Name: NameFull: Neuvéglise, Cécile – PersonEntity: Name: NameFull: Nicaud, Jean-Marc IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 09 Text: Sep2011 Type: published Y: 2011 Identifiers: – Type: issn-print Value: 01757598 Numbering: – Type: volume Value: 91 – Type: issue Value: 5 Titles: – TitleFull: Applied Microbiology & Biotechnology Type: main |
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