TY - JOUR
T1 - Chaperone complex formation of the transcription factor MalR involved in maltose utilization and amylolytic enzyme production in Aspergillus oryzae
AU - Konno, Yui
AU - Suzuki, Kuta
AU - Tanaka, Mizuki
AU - Shintani, Takahiro
AU - Gomi, Katsuya
N1 - Funding Information:
This work was supported by JSPS KAKENHI [grant number 25292044]; Program for Promotion of Basic and Applied Researches for Innovations in Bio-oriented Industry; and Science and Technology Research Promotion Program for Agriculture, Forestry, Fisheries and Food Industry.
Publisher Copyright:
© 2018 Japan society for Bioscience, Biotechnology, and agrochemistry.
PY - 2018
Y1 - 2018
N2 - The Zn2Cys6-type transcription factor MalR controls the expression of maltose-utilizing (MAL) cluster genes and the production of amylolytic enzymes in Aspergillus oryzae. In the present study, we demonstrated that MalR formed a complex with Hsp70 and Hsp90 chaperones under non-inducing conditions similar to the yeast counterpart Mal63 and that the complex was released from the chaperone complex after the addition of the inducer maltose. The MalR protein was constitutively localized in the nucleus and mutation in both the putative nuclear localization signals (NLSs) located in the zinc finger motif and the C-terminal region resulted in the loss of nuclear localization. This result indicated the involvement of NSLs in the MalR nuclear localization. However, mutation in both NLSs did not affect the dissociation mode of the MalR-Hsp70/Hsp90 complex, suggesting that MalR activation induced by maltose can occur regardless of its intracellular localization.
AB - The Zn2Cys6-type transcription factor MalR controls the expression of maltose-utilizing (MAL) cluster genes and the production of amylolytic enzymes in Aspergillus oryzae. In the present study, we demonstrated that MalR formed a complex with Hsp70 and Hsp90 chaperones under non-inducing conditions similar to the yeast counterpart Mal63 and that the complex was released from the chaperone complex after the addition of the inducer maltose. The MalR protein was constitutively localized in the nucleus and mutation in both the putative nuclear localization signals (NLSs) located in the zinc finger motif and the C-terminal region resulted in the loss of nuclear localization. This result indicated the involvement of NSLs in the MalR nuclear localization. However, mutation in both NLSs did not affect the dissociation mode of the MalR-Hsp70/Hsp90 complex, suggesting that MalR activation induced by maltose can occur regardless of its intracellular localization.
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U2 - 10.1080/09168451.2018.1447359
DO - 10.1080/09168451.2018.1447359
M3 - Article
C2 - 29517411
AN - SCOPUS:85046623981
VL - 82
SP - 827
EP - 835
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
SN - 0916-8451
IS - 5
ER -