Phylogenomic analysis of polyketide synthase genes in actinomycetes: structural analysis of KS domains and modules of polyketide synthases

2012 ◽  
Vol 5 (2) ◽  
pp. 89
Author(s):  
Samreen Sarwar ◽  
Mehboob Ahmed ◽  
Shahida Hasnain
Keyword(s):  
Structural Analysis ◽  
Polyketide Synthase ◽  
Polyketide Synthases ◽  
Phylogenomic Analysis

scholarly journals Engineered Biosynthesis of a Novel Amidated Polyketide, Using the Malonamyl-Specific Initiation Module from the Oxytetracycline Polyketide Synthase

2006 ◽  
Vol 72 (4) ◽  
pp. 2573-2580 ◽  
Author(s):  
Wenjun Zhang ◽  
Brian D. Ames ◽  
Shiou-Chuan Tsai ◽  
Yi Tang
Keyword(s):  
Polyketide Synthase ◽  
Major Product ◽  
Polyketide Synthases ◽  
Type Ii ◽  
Streptomyces Rimosus ◽  
Aromatic Polyketides ◽  
Starter Unit ◽  
Necessary And Sufficient ◽  
Bacterial Type

ABSTRACT Tetracyclines are aromatic polyketides biosynthesized by bacterial type II polyketide synthases (PKSs). Understanding the biochemistry of tetracycline PKSs is an important step toward the rational and combinatorial manipulation of tetracycline biosynthesis. To this end, we have sequenced the gene cluster of oxytetracycline (oxy and otc genes) PKS genes from Streptomyces rimosus. Sequence analysis revealed a total of 21 genes between the otrA and otrB resistance genes. We hypothesized that an amidotransferase, OxyD, synthesizes the malonamate starter unit that is a universal building block for tetracycline compounds. In vivo reconstitution using strain CH999 revealed that the minimal PKS and OxyD are necessary and sufficient for the biosynthesis of amidated polyketides. A novel alkaloid (WJ35, or compound 2) was synthesized as the major product when the oxy-encoded minimal PKS, the C-9 ketoreductase (OxyJ), and OxyD were coexpressed in CH999. WJ35 is an isoquinolone compound derived from an amidated decaketide backbone and cyclized with novel regioselectivity. The expression of OxyD with a heterologous minimal PKS did not afford similarly amidated polyketides, suggesting that the oxy-encoded minimal PKS possesses novel starter unit specificity.

Acyl Transferase Domains of Putative Polyketide Synthase (PKS) Genes in Aspergillus and Penicillium Producers of Ochratoxin A and the Evaluation of PCR Primers to Amplify PKS Sequences in Black Aspergillus Species

2009 ◽  
Vol 15 (1) ◽  
pp. 97-105 ◽  
Author(s):  
P.V. Martínez Culebras ◽  
A. Crespo-Sempere ◽  
J.V. Gil ◽  
D. Ramón
Keyword(s):  
Secondary Metabolites ◽  
Ochratoxin A ◽  
Polyketide Synthase ◽  
Pcr Primers ◽  
Polyketide Synthases ◽  
Aspergillus Species ◽  
Acyl Transferase ◽  
General Applicability ◽  
Phylogenetic Methods ◽  
Mycotoxin Biosynthesis

Fungal polyketide synthases (PKS) are responsible for the biosynthesis of several mycotoxins and other secondary metabolites. PKS genes in ochratoxin producing species from Aspergillus and Penicillum genera have been identified using a degenerate primer pair developed for the acyl transferase (AT) domain of fungal PKSs. Sequences of AT domains were aligned and analyzed using phylogenetic methods. The AT domain sequences appeared to be specific for a particular type of fungal PKSs and were related to PKSs involved in different mycotoxin biosynthesis pathways, including ochratoxin A. We have also developed primers suitable for amplifying AT domain sequences in strains belonging to the A. niger aggregate. DNA from most of the black Aspergillus species currently recognized was tested. Primers showed general applicability and other Aspergillus species belonging to section Nigri were successfully amplified.

scholarly journals Comparative Phylogenomic Analysis of Cytochrome P450 Monooxygenases From Fusarium Species

2021 ◽  
Author(s):  
Wadzani Palnam Dauda ◽  
Elkanah Glen ◽  
Peter Abraham ◽  
Charles Oluwaseun Adetunji ◽  
Daji Morumda ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Gene Cluster ◽  
Polyketide Synthase ◽  
Fusarium Species ◽  
Pathogenic Fungi ◽  
Plant Diseases ◽  
Biological Research ◽  
Cytochrome P450 Monooxygenases ◽  
Phylogenomic Analysis ◽  
P450 Monooxygenases

Abstract Cytochrome P450s (P450s) are a unique multifamily class of enzymes that possess the capability to exhibit catalytic versatility in several biochemical reactions which entails metabolite biosynthesis, primary and secondary metabolism. Fusarium spp. is an important microorganism with many members known to produce secondary metabolites that cause plant diseases and mycotoxicoses in animals and humans. In this present study, from the initially screened 4,579 proteins, we elucidated the nature of abundance, evolutionary relationships, classification and cellular location of 320 cytochrome P450 from 17 phytopathogenic members of Fusarium species. The total CYPs protein sequences were phylogenetically grouped into seventeen (17) clades. Eighty-six (86) CYPs families and forty-eight (48) clans were identified. Twenty-seven (27) families were each found in only one species. The CYPs were found to be majorly localized in the endoplasmic reticulum. The non-ribosomal peptide synthetase-like (NRPS-like) gene cluster was the predominant secondary metabolic-related gene cluster across all the seventeen selected Fusarium species except in F. cucurbiticola and F. solani, where PolyKetide Synthase (PKS) was the most prevalent. The presence of numerous families and clans as observed in in this study shows the expansions of the CYPs families across Fusarium species, this CYPs family and clan expansion is often associated with the evolvement of several fungal traits that include their pathogenicity adaptation to survive on an extensive range of toxic substrates. Identification of P450 proteins in these pathogenic fungi provides fundamental information for further basic and applied biological research into the physiological and toxigenic roles of P450s in Fusarium species.

scholarly journals Type II fatty acid and polyketide synthases: deciphering protein–protein and protein–substrate interactions

2018 ◽  
Vol 35 (10) ◽  
pp. 1029-1045 ◽  
Author(s):  
Aochiu Chen ◽  
Rebecca N. Re ◽  
Michael D. Burkart
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Synthase ◽  
Polyketide Synthase ◽  
Polyketide Synthases ◽  
Type Ii ◽  
Substrate Interactions ◽  
Protein Substrate ◽  
Functional Roles

Metabolites from type II fatty acid synthase (FAS) and polyketide synthase (PKS) pathways differ broadly in their identities and functional roles.

Computational Studies on the Substrate Specificity of an Acyltransferase Domain from Salinomycin Polyketide Synthase

2021 ◽  
Author(s):  
Huining Ji ◽  
Ting Shi ◽  
Lei Liu ◽  
Fa Zhang ◽  
Wentao Tao ◽  
...  
Keyword(s):  
Natural Products ◽  
Substrate Specificity ◽  
Polyketide Synthase ◽  
Coenzyme A ◽  
Biological Activities ◽  
Polyketide Synthases ◽  
Short Chain ◽  
Computational Studies ◽  
Chemical Structures ◽  
Coa Thioesters

Polyketides are a large group of natural products with diverse chemical structures and biological activities. They are biosynthesized by modular polyketide synthases (PKSs) from coenzyme A (CoA) thioesters of short-chain...

scholarly journals Polymorphism of the Polyketide Synthase Gene phlD in Biocontrol Fluorescent Pseudomonads Producing 2,4-Diacetylphloroglucinol and Comparison of PhlD with Plant Polyketide Synthases

2001 ◽  
Vol 14 (5) ◽  
pp. 639-652 ◽  
Author(s):  
Alban Ramette ◽  
Yvan Moënne-Loccoz ◽  
Geneviève Défago
Keyword(s):  
16S Rdna ◽  
Polyketide Synthase ◽  
Restriction Analysis ◽  
Polyketide Synthases ◽  
Fluorescent Pseudomonads ◽  
Phylogenetic Groups ◽  
Gram Positive ◽  
Restriction Patterns ◽  
Gram Positive Bacteria ◽  
Rdna Sequencing

Many biocontrol fluorescent pseudomonads can protect plants from soilborne fungal pathogens through production of the antifungal secondary metabolite 2,4-diacetylphloroglucinol (Phl). One of the phl biosynthetic genes, phlD, encodes a polyketide synthase similar to plant chalcone synthases. Here, restriction analysis of phlD from 39 Phl+ biocontrol fluorescent pseudomonads yielded seven different banding patterns. The gene was sequenced in seven strains, representing the different restriction patterns. Cluster analysis of phlD restriction data or phlD sequences indicated that phlD polymorphism was high, and two main clusters were obtained when predicted PhlD sequences were compared. When the seven PhlD sequences were studied with those of other procaryotic polyketide synthases (gram-positive bacteria) and plant chalcone synthases, however, Phl+ pseudomonads, gram-positive bacteria, and plants clustered separately. Yet, sequence analysis of active site regions for PhlD and plant chalcone synthases revealed that PhlD can be considered a member of the chalcone synthase family, which may be interpreted as convergent evolution of key enzymes involved in secondary metabolism. For the 39 Phl+ pseudomonads, a relationship was found among phlD restriction patterns, phylogenetic groups defined by 16S rDNA restriction analysis (confirmed by 16S rDNA sequencing), and production levels of Phl in vitro.

scholarly journals Phylogenetic and Structural Analysis of Polyketide Synthases inAspergilli

2016 ◽  
Vol 12 ◽  
pp. EBO.S32694 ◽  
Author(s):  
Preetida J. Bhetariya ◽  
Madhvi Prajapati ◽  
Asani Bhaduri ◽  
Rahul Shubhra Mandal ◽  
Anupam Varma ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Polyketide Synthases

Structural analysis of PKS1, a polyketide synthase gene involved in melanin biosynthesis in Colletotrichum lagenarium

1995 ◽  
Vol 249 (2) ◽  
pp. 162-167 ◽  
Author(s):  
Yoshitaka Takano ◽  
Yasuyuki Kubo ◽  
Kiminori Shimizu ◽  
Kazuyuki Mise ◽  
Tetsuro Okuno ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Polyketide Synthase ◽  
Colletotrichum Lagenarium ◽  
Melanin Biosynthesis ◽  
Polyketide Synthase Gene

scholarly journals Phylogenomic analysis of type I polyketide synthase genes in pathogenic and saprobic ascomycetes

2003 ◽  
Vol 100 (26) ◽  
pp. 15670-15675 ◽  
Author(s):  
S. Kroken ◽  
N. L. Glass ◽  
J. W. Taylor ◽  
O. C. Yoder ◽  
B. G. Turgeon
Keyword(s):  
Polyketide Synthase ◽  
Phylogenomic Analysis ◽  
Type I
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