Long-Chain Acyl-CoA Synthetase is Associated with the Growth of <i>Malassezia</i> spp.
The lipophilic fungal pathogen <i>Malassezia</i> spp. must acquire long-chain fatty acids (LCFAs) from outside the cell. To clarify the mechanism of LCFA acquisition, we investigated fatty acid uptake by this fungus and identified the long-chain acyl-CoA synthetase (ACS) gene <i>FA...
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MDPI AG
2019-09-01
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| Series: | Journal of Fungi |
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| Online Access: | https://www.mdpi.com/2309-608X/5/4/88 |
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| author | Tenagy Kengo Tejima Xinyue Chen Shun Iwatani Susumu Kajiwara |
| author_facet | Tenagy Kengo Tejima Xinyue Chen Shun Iwatani Susumu Kajiwara |
| author_sort | Tenagy |
| collection | DOAJ |
| description | The lipophilic fungal pathogen <i>Malassezia</i> spp. must acquire long-chain fatty acids (LCFAs) from outside the cell. To clarify the mechanism of LCFA acquisition, we investigated fatty acid uptake by this fungus and identified the long-chain acyl-CoA synthetase (ACS) gene <i>FAA1</i> in three <i>Malassezia</i> spp.: <i>M</i>. <i>globosa</i>, <i>M. pachydermatis</i>, and <i>M. sympodialis.</i> These <i>FAA1</i> genes could compensate for the double mutation of <i>FAA1</i> and <i>FAA4</i> in <i>Saccharomyces cerevisiae</i>, suggesting that <i>Malassezia</i> Faa1 protein recognizes exogenous LCFAs. <i>Mg</i>Faa1p and <i>Mp</i>Faa1p utilized a medium-chain fatty acid, lauric acid (C12:0). Interestingly, the ACS inhibitor, triacsin C, affected the activity of the <i>Malassezia</i> Faa1 proteins but not that of <i>S. cerevisiae</i>. Triacsin C also reduced the growth of <i>M. globosa</i>, <i>M. pachydermatis</i>, and <i>M. sympodialis</i>. These results suggest that triacsin C and its derivatives are potential compounds for the development of new anti-<i>Malassezia</i> drugs. |
| first_indexed | 2024-12-13T09:53:51Z |
| format | Article |
| id | doaj.art-1420e2977e454c288e5a901707cc48eb |
| institution | Directory Open Access Journal |
| issn | 2309-608X |
| language | English |
| last_indexed | 2024-12-13T09:53:51Z |
| publishDate | 2019-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Journal of Fungi |
| spelling | doaj.art-1420e2977e454c288e5a901707cc48eb2022-12-21T23:51:50ZengMDPI AGJournal of Fungi2309-608X2019-09-01548810.3390/jof5040088jof5040088Long-Chain Acyl-CoA Synthetase is Associated with the Growth of <i>Malassezia</i> spp.Tenagy0Kengo Tejima1Xinyue Chen2Shun Iwatani3Susumu Kajiwara4School of Life Science and Technology, Tokyo Institute of Technology, J3-7, 4259 Nagatsuta, Midori-ku, Yokohama, Kanagawa 226-8501, JapanSchool of Life Science and Technology, Tokyo Institute of Technology, J3-7, 4259 Nagatsuta, Midori-ku, Yokohama, Kanagawa 226-8501, JapanSchool of Life Science and Technology, Tokyo Institute of Technology, J3-7, 4259 Nagatsuta, Midori-ku, Yokohama, Kanagawa 226-8501, JapanSchool of Life Science and Technology, Tokyo Institute of Technology, J3-7, 4259 Nagatsuta, Midori-ku, Yokohama, Kanagawa 226-8501, JapanSchool of Life Science and Technology, Tokyo Institute of Technology, J3-7, 4259 Nagatsuta, Midori-ku, Yokohama, Kanagawa 226-8501, JapanThe lipophilic fungal pathogen <i>Malassezia</i> spp. must acquire long-chain fatty acids (LCFAs) from outside the cell. To clarify the mechanism of LCFA acquisition, we investigated fatty acid uptake by this fungus and identified the long-chain acyl-CoA synthetase (ACS) gene <i>FAA1</i> in three <i>Malassezia</i> spp.: <i>M</i>. <i>globosa</i>, <i>M. pachydermatis</i>, and <i>M. sympodialis.</i> These <i>FAA1</i> genes could compensate for the double mutation of <i>FAA1</i> and <i>FAA4</i> in <i>Saccharomyces cerevisiae</i>, suggesting that <i>Malassezia</i> Faa1 protein recognizes exogenous LCFAs. <i>Mg</i>Faa1p and <i>Mp</i>Faa1p utilized a medium-chain fatty acid, lauric acid (C12:0). Interestingly, the ACS inhibitor, triacsin C, affected the activity of the <i>Malassezia</i> Faa1 proteins but not that of <i>S. cerevisiae</i>. Triacsin C also reduced the growth of <i>M. globosa</i>, <i>M. pachydermatis</i>, and <i>M. sympodialis</i>. These results suggest that triacsin C and its derivatives are potential compounds for the development of new anti-<i>Malassezia</i> drugs.https://www.mdpi.com/2309-608X/5/4/88<i>Malassezia</i>acyl-CoA synthetasefatty acid uptake |
| spellingShingle | Tenagy Kengo Tejima Xinyue Chen Shun Iwatani Susumu Kajiwara Long-Chain Acyl-CoA Synthetase is Associated with the Growth of <i>Malassezia</i> spp. Journal of Fungi <i>Malassezia</i> acyl-CoA synthetase fatty acid uptake |
| title | Long-Chain Acyl-CoA Synthetase is Associated with the Growth of <i>Malassezia</i> spp. |
| title_full | Long-Chain Acyl-CoA Synthetase is Associated with the Growth of <i>Malassezia</i> spp. |
| title_fullStr | Long-Chain Acyl-CoA Synthetase is Associated with the Growth of <i>Malassezia</i> spp. |
| title_full_unstemmed | Long-Chain Acyl-CoA Synthetase is Associated with the Growth of <i>Malassezia</i> spp. |
| title_short | Long-Chain Acyl-CoA Synthetase is Associated with the Growth of <i>Malassezia</i> spp. |
| title_sort | long chain acyl coa synthetase is associated with the growth of i malassezia i spp |
| topic | <i>Malassezia</i> acyl-CoA synthetase fatty acid uptake |
| url | https://www.mdpi.com/2309-608X/5/4/88 |
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