TY - JOUR
T1 - Functional analysis of FarA transcription factor in the regulation of the genes encoding lipolytic enzymes and hydrophobic surface binding protein for the degradation of biodegradable plastics in Aspergillus oryzae
AU - Garrido, Sharon Marie
AU - Kitamoto, Noriyuki
AU - Watanabe, Akira
AU - Shintani, Takahiro
AU - Gomi, Katsuya
N1 - Funding Information:
We are grateful to Prof. Keietsu Abe for kindly providing the purified RolA protein and antibodies against RolA and HsbA. We also thank Drs. Mizuki Tanaka and Sachiko Shiro-Hasegawa for their helpful suggestions in the genetic manipulation of Aspergillus oryzae, and to Mr. Kimihide Muragaki for his technical assistance in the Western blot analysis. This study was supported in part by a Grant-in-Aid for Scientific Research on Priority Areas, Applied Genomics (no. 17019001 ), from the Ministry of Education, Culture, Sports, Science and Technology of Japan.
PY - 2012/5
Y1 - 2012/5
N2 - FarA is a Zn(II)2Cys6 transcription factor which upregulates genes required for growth on fatty acids in filamentous fungi like Aspergillus nidulans. FarA is also highly similar to the cutinase transcription factor CTF1α of Fusarium solani which binds to the cutinase gene promoter in this plant pathogen. This study determines whether FarA transcriptional factor also works in the regulation of genes responsible for the production of cutinase for the degradation of a biodegradable plastic, poly-(butylene succinate-co-adipate) (PBSA), in Aspergillus oryzae. The wild-type and the farA gene disruption strains were grown in minimal agar medium with emulsified PBSA, and the wild-type showed clear zone around the colonies while the disruptants did not. Western blot analysis revealed that the cutinase protein CutL1 and a hydrophobic surface binding protein such as HsbA were produced by the wild-type but not by the disruptants. In addition, the expressions of cutL1, triacylglycerol lipase (tglA), and mono- and di-acylglycerol lipase (mdlB) genes as well as the hsbA gene were significantly lower in the disruptants compared to the wild-type. These results indicated that the FarA transcriptional factor would be implicated in the expression of cutL1 and hsbA genes that are required for the degradation of PBSA as well as lipolytic genes such as mdlB and tglA for lipid hydrolysis.
AB - FarA is a Zn(II)2Cys6 transcription factor which upregulates genes required for growth on fatty acids in filamentous fungi like Aspergillus nidulans. FarA is also highly similar to the cutinase transcription factor CTF1α of Fusarium solani which binds to the cutinase gene promoter in this plant pathogen. This study determines whether FarA transcriptional factor also works in the regulation of genes responsible for the production of cutinase for the degradation of a biodegradable plastic, poly-(butylene succinate-co-adipate) (PBSA), in Aspergillus oryzae. The wild-type and the farA gene disruption strains were grown in minimal agar medium with emulsified PBSA, and the wild-type showed clear zone around the colonies while the disruptants did not. Western blot analysis revealed that the cutinase protein CutL1 and a hydrophobic surface binding protein such as HsbA were produced by the wild-type but not by the disruptants. In addition, the expressions of cutL1, triacylglycerol lipase (tglA), and mono- and di-acylglycerol lipase (mdlB) genes as well as the hsbA gene were significantly lower in the disruptants compared to the wild-type. These results indicated that the FarA transcriptional factor would be implicated in the expression of cutL1 and hsbA genes that are required for the degradation of PBSA as well as lipolytic genes such as mdlB and tglA for lipid hydrolysis.
KW - Aspergillus oryzae
KW - Cutinase
KW - Gene regulation
KW - Hydrophobic surface binding protein
KW - Lipolytic enzyme
KW - Transcription activator
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U2 - 10.1016/j.jbiosc.2011.12.014
DO - 10.1016/j.jbiosc.2011.12.014
M3 - Article
C2 - 22280964
AN - SCOPUS:84859885156
VL - 113
SP - 549
EP - 555
JO - Journal of Bioscience and Bioengineering
JF - Journal of Bioscience and Bioengineering
SN - 1389-1723
IS - 5
ER -