Thr/Ser-rich domain of Aspergillus glucoamylase is essential for secretion

Biosci Biotechnol Biochem. 2004 Apr;68(4):961-3. doi: 10.1271/bbb.68.961.

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

  • Aspergillus / drug effects
  • Aspergillus / enzymology*
  • Aspergillus / genetics
  • Fungal Proteins / genetics
  • Gene Expression Regulation / drug effects
  • Glucan 1,4-alpha-Glucosidase / chemistry*
  • Glucan 1,4-alpha-Glucosidase / genetics
  • Glucan 1,4-alpha-Glucosidase / metabolism*
  • HSP70 Heat-Shock Proteins / genetics
  • Maltose / pharmacology
  • Protein Structure, Tertiary
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Sequence Deletion / genetics
  • Serine / genetics
  • Serine / metabolism*
  • Threonine / genetics
  • Threonine / metabolism*

Substances

  • Fungal Proteins
  • HSP70 Heat-Shock Proteins
  • RNA, Messenger
  • Threonine
  • Serine
  • Maltose
  • Glucan 1,4-alpha-Glucosidase