Gibberellin Biosynthetic Pathway inGibberella fujikuroi:Evidence for a Gene Cluster

1998 ◽  
Vol 25 (3) ◽  
pp. 157-170 ◽  
Author(s):  
Bettina Tudzynski ◽  
Katja Hölter
Keyword(s):  
Gene Cluster ◽  
Biosynthetic Pathway

scholarly journals A Gene Cluster Containing Two Fungal Polyketide Synthases Encodes the Biosynthetic Pathway for a Polyketide, Asperfuranone, inAspergillus nidulans

2009 ◽  
Vol 131 (8) ◽  
pp. 2965-2970 ◽  
Author(s):  
Yi-Ming Chiang ◽  
Edyta Szewczyk ◽  
Ashley D. Davidson ◽  
Nancy Keller ◽  
Berl R. Oakley ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Biosynthetic Pathway ◽  
Polyketide Synthases

scholarly journals The fungal gene cluster for biosynthesis of the antibacterial agent viriditoxin

2019 ◽  
Author(s):  
Andrew S. Urquhart ◽  
Jinyu Hu ◽  
Yit-Heng Chooi ◽  
Alexander Idnurm
Keyword(s):  
Secondary Metabolites ◽  
Gene Cluster ◽  
Gene Disruption ◽  
Biosynthetic Pathway ◽  
Fluorescent Protein ◽  
Model Species ◽  
Paecilomyces Variotii ◽  
Bioinformatic Approaches ◽  
Green Fluorescent ◽  
Fungal Gene

AbstractBackgroundViriditoxin is one of the ‘classical’ secondary metabolites produced by fungi and that has antibacterial and other activities; however, the mechanism of its biosynthesis has remained unknown.ResultsHere, a gene cluster responsible for its synthesis was identified, using bioinformatic approaches from two species that produce viriditoxin and then through gene disruption and metabolite profiling. All eight genes in the cluster inPaecilomyces variotiiwere mutated, revealing their roles in the synthesis of this molecule and establishing its biosynthetic pathway which includes an interesting Baeyer-Villiger monooxygenase catalyzed reaction. Additionally, a candidate catalytically-inactive hydrolase was identified as being required for the stereoselective biosynthesis of (M)-viriditoxin. The localization of two proteins were assessed by fusing these proteins to green fluorescent protein, revealing that at least two intracellular structures are involved in the compartmentalization of the synthesis steps of this metabolite.ConclusionsThe full pathway for synthesis of viriditoxin was established by a combination of genomics, bioinformatics, gene disruption and chemical analysis processes. Hence, this work reveals the basis for the synthesis of an understudied class of fungal secondary metabolites and provides a new model species for understanding the synthesis of biaryl compounds with a chiral axis.

Biosynthesis of the uridine-derived nucleoside antibiotic A-94964: identification and characterization of the biosynthetic gene cluster provide insight into the biosynthetic pathway

2019 ◽  
Vol 17 (3) ◽  
pp. 461-466 ◽  
Author(s):  
Taro Shiraishi ◽  
Makoto Nishiyama ◽  
Tomohisa Kuzuyama
Keyword(s):  
Gene Cluster ◽  
In Silico ◽  
Biosynthetic Pathway ◽  
Gene Deletion ◽  
Biosynthetic Gene Cluster ◽  
Biosynthetic Gene ◽  
Identification And Characterization ◽  
Insight Into

The biosynthetic pathway of the uridine-derived nucleoside antibiotic A-94964 was proposed via in silico analysis coupled with gene deletion experiments.

scholarly journals Biosynthesis of Fusarubins Accounts for Pigmentation of Fusarium fujikuroi Perithecia

2012 ◽  
Vol 78 (12) ◽  
pp. 4468-4480 ◽  
Author(s):  
Lena Studt ◽  
Philipp Wiemann ◽  
Karin Kleigrewe ◽  
Hans-Ulrich Humpf ◽  
Bettina Tudzynski
Keyword(s):  
Secondary Metabolites ◽  
Gene Cluster ◽  
Biosynthetic Pathway ◽  
Polyketide Synthase ◽  
Biological Function ◽  
Fusarium Fujikuroi ◽  
Diverse Group ◽  
Fruiting Bodies ◽  
Content Type ◽  
Encoding Gene

ABSTRACTFusarium fujikuroiproduces a variety of secondary metabolites, of which polyketides form the most diverse group. Among these are the highly pigmented naphthoquinones, which have been shown to possess different functional properties for the fungus. A group of naphthoquinones, polyketides related to fusarubin, were identified inFusariumspp. more than 60 years ago, but neither the genes responsible for their formation nor their biological function has been discovered to date. In addition, although it is known that the sexual fruiting bodies in which the progeny of the fungus develops are darkly colored by a polyketide synthase (PKS)-derived pigment, the structure of this pigment has never been elucidated. Here we present data that link the fusarubin-type polyketides to a defined gene cluster, which we designatefsr, and demonstrate that the fusarubins are the pigments responsible for the coloration of the perithecia. We studied their regulation and the function of the single genes within the cluster by a combination of gene replacements and overexpression of the PKS-encoding gene, and we present a model for the biosynthetic pathway of the fusarubins based on these data.

A GENETIC AND BIOCHEMICAL STUDY OF HISTIDINE BIOSYNTHESIS IN MICROCOCCUS LUTEUS

Genetics ◽  
1975 ◽  
Vol 79 (3) ◽  
pp. 361-376
Author(s):  
Caroline Kane-Falce ◽  
Wesley E Kloos
Keyword(s):  
Gene Cluster ◽  
Biosynthetic Pathway ◽  
Gene Sequence ◽  
Biochemical Study ◽  
Micrococcus Luteus ◽  
Gene Clusters ◽  
Growth Responses ◽  
Histidine Biosynthesis ◽  
Marshall Test ◽  
Linkage Relationships

ABSTRACT Histidine auxotrophs of Micrococcus luteus strain ATCC 27141 were induced by treatment of the parent strain with N-methyl-N′-nitro-N-nitro-soguanidine. Auxotrophs were biochemically characterized by examining culture accumulations of histidine intermediates, using paper chromatography and the Bratton-Marshall test, and growth responses to L-histidinol. his(IG) mutants failed to accumulate Pauly-positive imidazoles; his(EAHF) mutants accumulated 5-amino-1-ribosyl-4-imidazole carboxamide; hisB mutants accumulated imidazoleglycerol; hisC mutants accumulated imidazoleacetol; hisD mutants accumulated histidinol. L-histidinol failed to stimulate the growth of hisD mutants, but did stimulate all other histidine mutants, blocked at earlier steps in the biosynthetic pathway. In addition, imidazoleglycerol phosphate dehydrase activity was assayed in representative mutants of each class. hisB mutants lacked activity for this enzyme.—Two-point, three-point, and cotransformation analyses resolved linkage relationships of histidine genes and in two gene clusters aided in determining their sequences. Histidine biosynthetic genes exist in at least four separate, unlinked regions of the chromosome. One histidine gene cluster is closely linked to a tryptophan gene cluster and appears to be contiguous in the sequence his(IG)-his(EAHF)-trpE-trpC-trpB-trpA. A second and unlinked histidine cluster has the tentative gene sequence his(EAHF)-hisB-hisC-his(EAHF). The hisD gene and an unclassified mutant site his-94 are not linked to any of the other histidine genes examined in this study or to each other.

scholarly journals Genetic Manipulation of the Fusarium fujikuroi Fusarin Gene Cluster Yields Insight into the Complex Regulation and Fusarin Biosynthetic Pathway

2013 ◽  
Vol 20 (8) ◽  
pp. 1055-1066 ◽  
Author(s):  
Eva-Maria Niehaus ◽  
Karin Kleigrewe ◽  
Philipp Wiemann ◽  
Lena Studt ◽  
Christian M.K. Sieber ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Biosynthetic Pathway ◽  
Genetic Manipulation ◽  
Fusarium Fujikuroi ◽  
Complex Regulation ◽  
Insight Into

scholarly journals Cloning and Characterization of the Biosynthetic Gene Cluster for Tomaymycin, an SJG-136 Monomeric Analog

2009 ◽  
Vol 75 (9) ◽  
pp. 2958-2963 ◽  
Author(s):  
Wei Li ◽  
ShenChieh Chou ◽  
Ankush Khullar ◽  
Barbara Gerratana
Keyword(s):  
Cluster Analysis ◽  
Gene Cluster ◽  
Biosynthetic Pathway ◽  
Biosynthetic Gene Cluster ◽  
Gene Replacement ◽  
Biosynthetic Gene

ABSTRACT Tomaymycin produced by Streptomyces achromogenes is a naturally produced pyrrolobenzodiazepine (PBD). The biosynthetic gene cluster for tomaymycin was identified and sequenced. The gene cluster analysis reveals a novel biosynthetic pathway for the anthranilate moiety of PBDs. Gene replacement and chemical complementation studies were used to confirm the proposed biosynthetic pathway.

scholarly journals Identification and Manipulation of the Caprazamycin Gene Cluster Lead to New Simplified Liponucleoside Antibiotics and Give Insights into the Biosynthetic Pathway

2009 ◽  
Vol 284 (22) ◽  
pp. 14987-14996 ◽  
Author(s):  
Leonard Kaysser ◽  
Liane Lutsch ◽  
Stefanie Siebenberg ◽  
Emmanuel Wemakor ◽  
Bernd Kammerer ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Biosynthetic Pathway

scholarly journals Biosynthetic Pathway for γ-Cyclic Sarcinaxanthin in Micrococcus luteus: Heterologous Expression and Evidence for Diverse and Multiple Catalytic Functions of C50 Carotenoid Cyclases

2010 ◽  
Vol 192 (21) ◽  
pp. 5688-5699 ◽  
Author(s):  
Roman Netzer ◽  
Marit H. Stafsnes ◽  
Trygve Andreassen ◽  
Audun Goksøyr ◽  
Per Bruheim ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Biosynthetic Pathway ◽  
Micrococcus Luteus ◽  
Dry Weight ◽  
Biosynthetic Gene Cluster ◽  
Hybrid Gene ◽  
E Coli ◽  
Shake Flasks ◽  
Catalytic Functions ◽  
First Time

ABSTRACT We report the cloning and characterization of the biosynthetic gene cluster (crtE, crtB, crtI, crtE2, crtYg, crtYh, and crtX) of the γ-cyclic C50 carotenoid sarcinaxanthin in Micrococcus luteus NCTC2665. Expression of the complete and partial gene cluster in Escherichia coli hosts revealed that sarcinaxanthin biosynthesis from the precursor molecule farnesyl pyrophosphate (FPP) proceeds via C40 lycopene, C45 nonaflavuxanthin, C50 flavuxanthin, and C50 sarcinaxanthin. Glucosylation of sarcinaxanthin was accomplished by the crtX gene product. This is the first report describing the biosynthetic pathway of a γ-cyclic C50 carotenoid. Expression of the corresponding genes from the marine M. luteus isolate Otnes7 in a lycopene-producing E. coli host resulted in the production of up to 2.5 mg/g cell dry weight sarcinaxanthin in shake flasks. In an attempt to experimentally understand the specific difference between the biosynthetic pathways of sarcinaxanthin and the structurally related ε-cyclic decaprenoxanthin, we constructed a hybrid gene cluster with the γ-cyclic C50 carotenoid cyclase genes crtYg and crtYh from M. luteus replaced with the analogous ε-cyclic C50 carotenoid cyclase genes crtYe and crtYf from the natural decaprenoxanthin producer Corynebacterium glutamicum. Surprisingly, expression of this hybrid gene cluster in an E. coli host resulted in accumulation of not only decaprenoxanthin, but also sarcinaxanthin and the asymmetric ε- and γ-cyclic C50 carotenoid sarprenoxanthin, described for the first time in this work. Together, these data contributed to new insight into the diverse and multiple functions of bacterial C50 carotenoid cyclases as key catalysts for the synthesis of structurally different carotenoids.

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