Heterologous expression of highly reducing polyketide synthase involved in betaenone biosynthesis

2015 ◽  
Vol 51 (10) ◽  
pp. 1878-1881 ◽  
Author(s):  
Takahiro Ugai ◽  
Atsushi Minami ◽  
Ryuya Fujii ◽  
Mizuki Tanaka ◽  
Hiroki Oguri ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Polyketide Synthase ◽  
Enoyl Reductase

Heterologous expression of highly reducing polyketide synthase and trans-acting enoyl reductase provides insights into the skeletal construction of betaenones.

scholarly journals The PKS4 Gene of Fusarium graminearum Is Essential for Zearalenone Production

2006 ◽  
Vol 72 (6) ◽  
pp. 3924-3932 ◽  
Author(s):  
Erik Lys�e ◽  
Sonja S. Klemsdal ◽  
Karen R. Bone ◽  
Rasmus J. N. Frandsen ◽  
Thomas Johansen ◽  
...  
Keyword(s):  
Fusarium Graminearum ◽  
High Performance ◽  
Polyketide Synthase ◽  
Wild Type ◽  
Root Infection ◽  
Enoyl Reductase ◽  
Transformation Protocol ◽  
Chromatography Analysis ◽  
In The Wild ◽  
High Level

ABSTRACT Zearalenones are produced by several Fusarium species and can cause reproductive problems in animals. Some aurofusarin mutants of Fusarium pseudograminearum produce elevated levels of zearalenone (ZON), one of the estrogenic mycotoxins comprising the zearalenones. An analysis of transcripts from polyketide synthase genes identified in the Fusarium graminearum database was carried out for these mutants. PKS4 was the only gene with an enoyl reductase domain that had a higher level of transcription in the aurofusarin mutants than in the wild type. An Agrobacterium tumefaciens-mediated transformation protocol was used to replace the central part of the PKS4 gene with a hygB resistance gene through double homologous recombination in an F. graminearum strain producing a high level of ZON. PCR and Southern analysis of transformants were used to identify isolates with single insertional replacements of PKS4. High-performance liquid chromatography analysis showed that the PKS4 replacement mutant did not produce ZON. Thus, PKS4 encodes an enzyme required for the production of ZON in F. graminearum. Barley root infection studies revealed no alteration in the pathogenicity of the PKS4 mutant compared to the pathogenicity of the wild type. The expression of PKS13, which is located in the same cluster as PKS4, decreased dramatically in the mutant, while transcription of PKS4 was unchanged. This differential expression may indicate that ZON or its derivatives do not regulate expression of PKS4 and that the PKS4-encoded protein or its product stimulates expression of PKS13. Furthermore, both the lack of aurofusarin and ZON influenced the expression of other polyketide synthases, demonstrating that one polyketide can influence the expression of others.

scholarly journals Reengineering the programming of a functional domain of an iterative highly reducing polyketide synthase

RSC Advances ◽  
2020 ◽  
Vol 10 (31) ◽  
pp. 18469-18476
Author(s):  
Oliver Piech ◽  
Russell J. Cox
Keyword(s):  
Polyketide Synthase ◽  
Functional Domain ◽  
Enoyl Reductase ◽  
Directed Mutation ◽  
First Time ◽  
Intrinsic Program

Site-directed mutation of the enoyl reductase (ER) component of an iterative highly-reducing polyketide synthase was achieved for the first time, expanding its intrinsic program.

scholarly journals Engineering Fungal Nonreducing Polyketide Synthase by Heterologous Expression and Domain Swapping

2013 ◽  
Vol 15 (4) ◽  
pp. 756-759 ◽  
Author(s):  
Hsu-Hua Yeh ◽  
Shu-Lin Chang ◽  
Yi-Ming Chiang ◽  
Kenneth S. Bruno ◽  
Berl R. Oakley ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Polyketide Synthase ◽  
Domain Swapping

scholarly journals Substrate selectivity of an isolated enoyl reductase catalytic domain from an iterative highly reducing fungal polyketide synthase reveals key components of programming

2017 ◽  
Vol 8 (2) ◽  
pp. 1116-1126 ◽  
Author(s):  
Douglas M. Roberts ◽  
Christoph Bartel ◽  
Alan Scott ◽  
David Ivison ◽  
Thomas J. Simpson ◽  
...  
Keyword(s):  
Polyketide Synthase ◽  
Catalytic Domain ◽  
Substrate Selectivity ◽  
Enoyl Reductase ◽  
Reductase Domain

The complete stereochemical course and substrate selectivity of the enoyl reductase domain from the fungal polyketide synthase squalestatin tetraketide synthase (SQTKS) have been determined.

scholarly journals Discovery and biosynthesis of clostyrylpyrones from the obligate anaerobe Clostridium roseum

2020 ◽  
Author(s):  
Jeffrey S Li ◽  
Yongle Du ◽  
Di Gu ◽  
Wenlong Cai ◽  
Allison Green ◽  
...  
Keyword(s):  
Natural Products ◽  
Heterologous Expression ◽  
Natural Product ◽  
Biochemical Analysis ◽  
Polyketide Synthase ◽  
Gene Knockout ◽  
Anaerobic Bacteria ◽  
Obligate Anaerobe ◽  
New Family ◽  
Expression Studies

ABSTRACTAnaerobic bacteria are a promising new source for natural product discovery. Examination of extracts from the obligate anaerobe Clostridium roseum led to discovery of a new family of natural products, the clostyrylpyrones. The polyketide synthase-based biosynthetic mechanism of clostyrylpyrones is further proposed based on bioinformatic, gene knockout, biochemical analysis and heterologous expression studies.

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