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| [PMID]: | 28455339 |
| [Au] Autor: | Tanaka M; Hiramoto T; Tada H; Shintani T; Gomi K |
| [Ad] Endereço: | Laboratory of Bioindustrial Genomics, Department of Bioindustrial Informatics and Genomics, Graduate School of Agricultural Science, Tohoku University, Aramaki, Aoba-ku, Sendai, Japan. |
| [Ti] Título: | Improved α-Amylase Production by Dephosphorylation Mutation of CreD, an Arrestin-Like Protein Required for Glucose-Induced Endocytosis of Maltose Permease and Carbon Catabolite Derepression in Aspergillus oryzae. |
| [So] Source: | Appl Environ Microbiol;83(13), 2017 Jul 01. | | [Is] ISSN: | 1098-5336 |
| [Cp] País de publicação: | United States |
| [La] Idioma: | eng |
| [Ab] Resumo: | produces copious amount of amylolytic enzymes, and MalP, a major maltose permease, is required for the expression of amylase-encoding genes. The expression of these genes is strongly repressed by carbon catabolite repression (CCR) in the presence of glucose. MalP is transported from the plasma membrane to the vacuole by endocytosis, which requires the homolog of E6-AP carboxyl terminus ubiquitin ligase HulA, an ortholog of yeast Rsp5. In yeast, arrestin-like proteins mediate endocytosis as adaptors of Rsp5 and transporters. In the present study, we examined the involvement of CreD, an arrestin-like protein, in glucose-induced MalP endocytosis and CCR of amylase-encoding genes. Deletion of inhibited the glucose-induced endocytosis of MalP, and CreD showed physical interaction with HulA. Phosphorylation of CreD was detected by Western blotting, and two serine residues were determined as the putative phosphorylation sites. However, the phosphorylation state of the serine residues did not regulate MalP endocytosis and its interaction with HulA. Although α-amylase production was significantly repressed by deletion, both phosphorylation and dephosphorylation mimics of CreD had a negligible effect on α-amylase activity. Interestingly, dephosphorylation of CreD was required for CCR relief of amylase genes that was triggered by disruption of the deubiquitinating enzyme-encoding gene The α-amylase activity of the mutant was 1.6-fold higher than that of the wild type, and the dephosphorylation mimic of CreD further improved the α-amylase activity by 2.6-fold. These results indicate that a combination of the dephosphorylation mutation of CreD and disruption increased the production of amylolytic enzymes in In eukaryotes, glucose induces carbon catabolite repression (CCR) and proteolytic degradation of plasma membrane transporters via endocytosis. Glucose-induced endocytosis of transporters is mediated by their ubiquitination, and arrestin-like proteins act as adaptors of transporters and ubiquitin ligases. In this study, we showed that CreD, an arrestin-like protein, is involved in glucose-induced endocytosis of maltose permease and carbon catabolite derepression of amylase gene expression in Dephosphorylation of CreD was required for CCR relief triggered by the disruption of , which encodes a deubiquitinating enzyme; a combination of the phosphorylation-defective mutation of CreD and disruption dramatically improved α-amylase production. This study shows the dual function of an arrestin-like protein and provides a novel approach for improving the production of amylolytic enzymes in . |
| [Mh] Termos MeSH primário: |
Arrestina/metabolismo
Aspergillus oryzae/metabolismo
Repressão Catabólica
Endocitose
Proteínas Fúngicas/genética
Proteínas de Transporte de Monossacarídeos/genética
alfa-Amilases/genética
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| [Mh] Termos MeSH secundário: |
Arrestina/genética
Aspergillus oryzae/enzimologia
Aspergillus oryzae/genética
Carbono/metabolismo
Proteínas Fúngicas/metabolismo
Regulação Fúngica da Expressão Gênica
Glucose/metabolismo
Proteínas de Transporte de Monossacarídeos/metabolismo
Mutação
Fosforilação
Transporte Proteico
alfa-Amilases/metabolismo
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| [Pt] Tipo de publicação: | JOURNAL ARTICLE |
[Nm] Nome de substância:
| 0 (Arrestin); 0 (Fungal Proteins); 0 (Monosaccharide Transport Proteins); 7440-44-0 (Carbon); 9055-23-6 (maltose permease); EC 3.2.1.1 (alpha-Amylases); IY9XDZ35W2 (Glucose) |
| [Em] Mês de entrada: | 1712 |
| [Cu] Atualização por classe: | 171225 |
[Lr] Data última revisão:
| 171225 |
| [Sb] Subgrupo de revista: | IM |
| [Da] Data de entrada para processamento: | 170430 |
| [St] Status: | MEDLINE |
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