Identification of an Acidic Amino Acid Permease Involved in <span style="font-variant: small-caps">d-</span>Aspartate Uptake in the Yeast <i>Cryptococcus humicola</i>
<span style="font-variant: small-caps;">d-</span>aspartate oxidase (DDO) catalyzes the oxidative deamination of acidic <span style="font-variant: small-caps;">d-</span>amino acids, and its production is induced by <span style="font-variant: small-c...
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MDPI AG
2021-01-01
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| Series: | Microorganisms |
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| Online Access: | https://www.mdpi.com/2076-2607/9/1/192 |
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| author | Daiki Imanishi Yoshio Kera Shouji Takahashi |
| author_facet | Daiki Imanishi Yoshio Kera Shouji Takahashi |
| author_sort | Daiki Imanishi |
| collection | DOAJ |
| description | <span style="font-variant: small-caps;">d-</span>aspartate oxidase (DDO) catalyzes the oxidative deamination of acidic <span style="font-variant: small-caps;">d-</span>amino acids, and its production is induced by <span style="font-variant: small-caps;">d-</span>Asp in several eukaryotes. The yeast <i>Cryptococcus humicola</i> strain UJ1 produces large amounts of DDO (ChDDO) only in the presence of <span style="font-variant: small-caps;">d-</span>Asp. In this study, we analyzed the relationship between <span style="font-variant: small-caps;">d-</span>Asp uptake by an amino acid permease (Aap) and the inducible expression of ChDDO. We identified two acidic Aap homologs, named “ChAap4 and ChAap5,” in the yeast genome sequence. <i>ChAAP4</i> deletion resulted in partial growth defects on <span style="font-variant: small-caps;">d-</span>Asp as well as <span style="font-variant: small-caps;">l-</span>Asp, <span style="font-variant: small-caps;">l-</span>Glu, and <span style="font-variant: small-caps;">l-</span>Phe at pH 7, whereas <i>ChAAP5</i> deletion caused partial growth defects on <span style="font-variant: small-caps;">l-</span>Phe and <span style="font-variant: small-caps;">l-</span>Lys, suggesting that ChAap4 might participate in <span style="font-variant: small-caps;">d-</span>Asp uptake as an acidic Aap. Interestingly, the growth of the <i>Chaap4</i> strain on <span style="font-variant: small-caps;">d-</span> or <span style="font-variant: small-caps;">l-</span>Asp was completely abolished at pH 10, suggesting that ChAap4 is the only Aap responsible for <span style="font-variant: small-caps;">d-</span> and <span style="font-variant: small-caps;">l-</span>Asp uptake under high alkaline conditions. In addition, <i>ChAAP4</i> deletion significantly decreased the induction of DDO activity and <i>ChDDO</i> transcription in the presence of <span style="font-variant: small-caps;">d-</span>Asp. This study revealed that <span style="font-variant: small-caps;">d-</span>Asp uptake by ChAap4 might be involved in the induction of <i>ChDDO</i> expression by <span style="font-variant: small-caps;">d-</span>Asp. |
| first_indexed | 2024-03-09T04:27:21Z |
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| last_indexed | 2024-03-09T04:27:21Z |
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| spelling | doaj.art-f2520dbf6b804d50af197a795a688baf2023-12-03T13:39:43ZengMDPI AGMicroorganisms2076-26072021-01-019119210.3390/microorganisms9010192Identification of an Acidic Amino Acid Permease Involved in <span style="font-variant: small-caps">d-</span>Aspartate Uptake in the Yeast <i>Cryptococcus humicola</i>Daiki Imanishi0Yoshio Kera1Shouji Takahashi2Department of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, JapanDepartment of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, JapanDepartment of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan<span style="font-variant: small-caps;">d-</span>aspartate oxidase (DDO) catalyzes the oxidative deamination of acidic <span style="font-variant: small-caps;">d-</span>amino acids, and its production is induced by <span style="font-variant: small-caps;">d-</span>Asp in several eukaryotes. The yeast <i>Cryptococcus humicola</i> strain UJ1 produces large amounts of DDO (ChDDO) only in the presence of <span style="font-variant: small-caps;">d-</span>Asp. In this study, we analyzed the relationship between <span style="font-variant: small-caps;">d-</span>Asp uptake by an amino acid permease (Aap) and the inducible expression of ChDDO. We identified two acidic Aap homologs, named “ChAap4 and ChAap5,” in the yeast genome sequence. <i>ChAAP4</i> deletion resulted in partial growth defects on <span style="font-variant: small-caps;">d-</span>Asp as well as <span style="font-variant: small-caps;">l-</span>Asp, <span style="font-variant: small-caps;">l-</span>Glu, and <span style="font-variant: small-caps;">l-</span>Phe at pH 7, whereas <i>ChAAP5</i> deletion caused partial growth defects on <span style="font-variant: small-caps;">l-</span>Phe and <span style="font-variant: small-caps;">l-</span>Lys, suggesting that ChAap4 might participate in <span style="font-variant: small-caps;">d-</span>Asp uptake as an acidic Aap. Interestingly, the growth of the <i>Chaap4</i> strain on <span style="font-variant: small-caps;">d-</span> or <span style="font-variant: small-caps;">l-</span>Asp was completely abolished at pH 10, suggesting that ChAap4 is the only Aap responsible for <span style="font-variant: small-caps;">d-</span> and <span style="font-variant: small-caps;">l-</span>Asp uptake under high alkaline conditions. In addition, <i>ChAAP4</i> deletion significantly decreased the induction of DDO activity and <i>ChDDO</i> transcription in the presence of <span style="font-variant: small-caps;">d-</span>Asp. This study revealed that <span style="font-variant: small-caps;">d-</span>Asp uptake by ChAap4 might be involved in the induction of <i>ChDDO</i> expression by <span style="font-variant: small-caps;">d-</span>Asp.https://www.mdpi.com/2076-2607/9/1/192<span style="font-variant: small-caps">d-</span>aspartate oxidaseamino acid permease<i>Cryptococcus humicola</i><span style="font-variant: small-caps">d</span>-aspartategene expression |
| spellingShingle | Daiki Imanishi Yoshio Kera Shouji Takahashi Identification of an Acidic Amino Acid Permease Involved in <span style="font-variant: small-caps">d-</span>Aspartate Uptake in the Yeast <i>Cryptococcus humicola</i> Microorganisms <span style="font-variant: small-caps">d-</span>aspartate oxidase amino acid permease <i>Cryptococcus humicola</i> <span style="font-variant: small-caps">d</span>-aspartate gene expression |
| title | Identification of an Acidic Amino Acid Permease Involved in <span style="font-variant: small-caps">d-</span>Aspartate Uptake in the Yeast <i>Cryptococcus humicola</i> |
| title_full | Identification of an Acidic Amino Acid Permease Involved in <span style="font-variant: small-caps">d-</span>Aspartate Uptake in the Yeast <i>Cryptococcus humicola</i> |
| title_fullStr | Identification of an Acidic Amino Acid Permease Involved in <span style="font-variant: small-caps">d-</span>Aspartate Uptake in the Yeast <i>Cryptococcus humicola</i> |
| title_full_unstemmed | Identification of an Acidic Amino Acid Permease Involved in <span style="font-variant: small-caps">d-</span>Aspartate Uptake in the Yeast <i>Cryptococcus humicola</i> |
| title_short | Identification of an Acidic Amino Acid Permease Involved in <span style="font-variant: small-caps">d-</span>Aspartate Uptake in the Yeast <i>Cryptococcus humicola</i> |
| title_sort | identification of an acidic amino acid permease involved in span style font variant small caps d span aspartate uptake in the yeast i cryptococcus humicola i |
| topic | <span style="font-variant: small-caps">d-</span>aspartate oxidase amino acid permease <i>Cryptococcus humicola</i> <span style="font-variant: small-caps">d</span>-aspartate gene expression |
| url | https://www.mdpi.com/2076-2607/9/1/192 |
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