Two novel classes of enzymes are required for the biosynthesis of aurofusarin in Fusarium graminearum.
(2011) In Journal of Biological Chemistry- Abstract
- Previous studies have reported the functional characterization of nine out of eleven genes found in the gene cluster responsible for biosynthesis of the polyketide pigment aurofusarin in Fusarium graminearum. Here we reanalyse the function of a putative aurofusarin pump (AurT) and the two remaining orphan genes, aurZ and aurS. Targeted gene replacement of aurZ resulted in the discovery that the compound YWA1, rather than nor-rubrofusarin, is the primary product of F. graminearum polyketide synthase 12 (FgPKS12). AurZ is the first representative of a novel class of dehydratases that act on hydroxylated γ-pyrones. Replacement of the aurS gene resulted in accumulation of rubrofusarin, an intermediate that also accumulates when the GIP1, aurF... (More)
- Previous studies have reported the functional characterization of nine out of eleven genes found in the gene cluster responsible for biosynthesis of the polyketide pigment aurofusarin in Fusarium graminearum. Here we reanalyse the function of a putative aurofusarin pump (AurT) and the two remaining orphan genes, aurZ and aurS. Targeted gene replacement of aurZ resulted in the discovery that the compound YWA1, rather than nor-rubrofusarin, is the primary product of F. graminearum polyketide synthase 12 (FgPKS12). AurZ is the first representative of a novel class of dehydratases that act on hydroxylated γ-pyrones. Replacement of the aurS gene resulted in accumulation of rubrofusarin, an intermediate that also accumulates when the GIP1, aurF or aurO genes in the aurofusarin cluster are deleted. Based on the shared phenotype and predicted subcellular localization we propose that AurS is a member of an extracellular enzyme complex (GIP1-AurF-AurO-AurS) responsible for converting rubrofusarin into aurofusarin. This implies that rubrofusarin, rather than aurofusarin, is pumped across the plasma membrane. Replacement of the putative aurofusarin pump aurT increased rubrofusarin to aurofusarin ratio, supporting that rubrofusarin is normally pumped across the plasma membrane. These results provide functional information on two novel classes of proteins and their contribution to polyketide pigment biosynthesis. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1832248
- author
- Frandsen, Rasmus J N ; Schutt, Claes ; Lund, Birgitte W ; Staerk, Dan ; Nielsen, John ; Olsson Hau, Stefan LU and Giese, Henriette
- organization
- publishing date
- 2011-02-04
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:21296881
- scopus:79953188685
- pmid:21296881
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.M110.179853
- language
- English
- LU publication?
- yes
- id
- 6b1372fe-808f-46a3-932c-f2c754a562a2 (old id 1832248)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/21296881?dopt=Abstract
- date added to LUP
- 2016-04-04 08:53:57
- date last changed
- 2022-04-08 00:34:16
@article{6b1372fe-808f-46a3-932c-f2c754a562a2, abstract = {{Previous studies have reported the functional characterization of nine out of eleven genes found in the gene cluster responsible for biosynthesis of the polyketide pigment aurofusarin in Fusarium graminearum. Here we reanalyse the function of a putative aurofusarin pump (AurT) and the two remaining orphan genes, aurZ and aurS. Targeted gene replacement of aurZ resulted in the discovery that the compound YWA1, rather than nor-rubrofusarin, is the primary product of F. graminearum polyketide synthase 12 (FgPKS12). AurZ is the first representative of a novel class of dehydratases that act on hydroxylated γ-pyrones. Replacement of the aurS gene resulted in accumulation of rubrofusarin, an intermediate that also accumulates when the GIP1, aurF or aurO genes in the aurofusarin cluster are deleted. Based on the shared phenotype and predicted subcellular localization we propose that AurS is a member of an extracellular enzyme complex (GIP1-AurF-AurO-AurS) responsible for converting rubrofusarin into aurofusarin. This implies that rubrofusarin, rather than aurofusarin, is pumped across the plasma membrane. Replacement of the putative aurofusarin pump aurT increased rubrofusarin to aurofusarin ratio, supporting that rubrofusarin is normally pumped across the plasma membrane. These results provide functional information on two novel classes of proteins and their contribution to polyketide pigment biosynthesis.}}, author = {{Frandsen, Rasmus J N and Schutt, Claes and Lund, Birgitte W and Staerk, Dan and Nielsen, John and Olsson Hau, Stefan and Giese, Henriette}}, issn = {{1083-351X}}, language = {{eng}}, month = {{02}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{Two novel classes of enzymes are required for the biosynthesis of aurofusarin in Fusarium graminearum.}}, url = {{http://dx.doi.org/10.1074/jbc.M110.179853}}, doi = {{10.1074/jbc.M110.179853}}, year = {{2011}}, }