Abstract
The recombinant Aspergillus awamori strain carrying the mutant glucoamylase-encoding gene in which the entire Thr/Ser-rich Gp-I domain was deleted abolished secretion of mutant glucoamylase. The transcription of the Bip-encoding bipA was low in the wild type (wt) strain, but elevated in the recombinant strain under the condition of glaA expression. The results indicate that the Gp-I domain is vital for glucoamylase secretion.
MeSH terms
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Aspergillus / drug effects
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Aspergillus / enzymology*
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Aspergillus / genetics
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Fungal Proteins / genetics
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Gene Expression Regulation / drug effects
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Glucan 1,4-alpha-Glucosidase / chemistry*
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Glucan 1,4-alpha-Glucosidase / genetics
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Glucan 1,4-alpha-Glucosidase / metabolism*
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HSP70 Heat-Shock Proteins / genetics
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Maltose / pharmacology
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Protein Structure, Tertiary
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Sequence Deletion / genetics
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Serine / genetics
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Serine / metabolism*
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Threonine / genetics
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Threonine / metabolism*
Substances
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Fungal Proteins
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HSP70 Heat-Shock Proteins
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RNA, Messenger
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Threonine
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Serine
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Maltose
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Glucan 1,4-alpha-Glucosidase