Thr/Ser-rich domain of Aspergillus glucoamylase is essential for secretion.
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.
Goto
Masatoshi
M
Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Hakozaki, Fukuoka, Japan. m_goto@agr.kyushu-u.ac.jp
Shinoda
Noriko
N
Oka
Takuji
T
Sameshima
Yuka
Y
Ekino
Keisuke
K
Furukawa
Kensuke
K
D001230:Aspergillus / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D005656:Fungal Proteins / Q000235:genetics; D005786:Gene Expression Regulation / Q000187:drug effects; D005087:Glucan 1,4-alpha-Glucosidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics; D008320:Maltose / Q000494:pharmacology; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion / Q000235:genetics; D012694:Serine / Q000235:genetics / Q000378:metabolism*; D013912:Threonine / Q000235:genetics / Q000378:metabolism*
D005656:Fungal Proteins; D018840:HSP70 Heat-Shock Proteins; D012333:RNA, Messenger; D013912:Threonine; D012694:Serine; D008320:Maltose; D005087:Glucan 1,4-alpha-Glucosidase