ArticleThe Journal of biological chemistry2014
Fatty aldehyde dehydrogenase multigene family involved in the assimilation of n-alkanes in Yarrowia lipolytica.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 45 citations in OpenAlex.
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- Phosphatidylserine synthase plays a critical role in the utilization of n-alkanes in the yeast Yarrowia lipolytica.FEMS yeast research · 2024Article
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- Bioengineering for the Microbial Degradation of Petroleum Hydrocarbon Contaminants.Bioengineering (Basel, Switzerland) · 2023Review
- Utilization of n-alkane and roles of lipid transfer proteins in Yarrowia lipolytica.World journal of microbiology & biotechnology · 2023Review
- Improving Lipid Production ofInternational journal of molecular sciences · 2022Article
- Extrapolation of design strategies for lignocellulosic biomass conversion to the challenge of plastic waste.Journal of industrial microbiology & biotechnology · 2022Article
- Engineering the oleaginous yeastBiotechnology for biofuels · 2019Article
- Multi-Omics Analysis of Fatty Alcohol Production in Engineered YeastsFrontiers in genetics · 2019Article
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- Integrating Cellular and Bioprocess Engineering in the Non-Conventional YeastFrontiers in bioengineering and biotechnology · 2017Review
- Exploring fatty alcohol-producing capability of Yarrowia lipolytica.Biotechnology for biofuels · 2016Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
In the n-alkane assimilating yeast Yarrowia lipolytica, n-alkanes are oxidized to fatty acids via fatty alcohols and fatty aldehydes, after which they are utilized as carbon sources. Here, we show that four genes (HFD1-HFD4) encoding fatty aldehyde dehydrogenases (FALDHs) are involved in the metabolism of n-alkanes in Y. lipolytica. A mutant, in which all of four HFD genes are deleted (Δhfd1-4 strain), could not grow on n-alkanes of 12-18 carbons; however, the expression of one of those HFD genes restored its growth on n-alkanes. Production of Hfd2Ap or Hfd2Bp, translation products of transcript variants generated from HFD2 by the absence or presence of splicing, also supported the growth of the Δhfd1-4 strain on n-alkanes. The FALDH activity in the extract of the wild-type strain was increased when cells were incubated in the presence of n-decane, whereas this elevation in FALDH activity by n-decane was not observed in Δhfd1-4 strain extract. Substantial FALDH activities were detected in the extracts of Escherichia coli cells expressing the HFD genes. Fluorescent microscopic observation suggests that Hfd3p and Hfd2Bp are localized predominantly in the peroxisome, whereas Hfd1p and Hfd2Ap are localized in both the endoplasmic reticulum and the peroxisome. These results suggest that the HFD multigene family is responsible for the oxidation of fatty aldehydes to fatty acids in the metabolism of n-alkanes, and raise the possibility that Hfd proteins have diversified by gene multiplication and RNA splicing to efficiently assimilate or detoxify fatty aldehydes in Y. lipolytica.
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