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Correction for Wang et al., Unraveling the iterative type I polyketide synthases hidden in Streptomyces.

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PROVIDER: S-EPMC8719864 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature

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Correction for Wang et al., Unraveling the iterative type I polyketide synthases hidden in Streptomyces.

Proceedings of the National Academy of Sciences of the United States of America 20211201 52

PMID: 34949643

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Unraveling the iterative type I polyketide synthases hidden in Streptomyces.

Project description:Type I polyketide synthases (T1PKSs) are one of the most extensively studied PKSs, which can act either iteratively or via an assembly-line mechanism. Domains in the T1PKSs can readily be predicted by computational tools based on their highly conserved sequences. However, to distinguish between iterative and noniterative at the module level remains an overwhelming challenge, which may account for the seemingly biased distribution of T1PKSs in fungi and bacteria: small iterative monomodular T1PKSs that are responsible for the enormously diverse fungal natural products exist almost exclusively in fungi. Here we report the discovery of iterative T1PKSs that are unexpectedly both abundant and widespread in Streptomyces Seven of 11 systematically selected T1PKS monomodules from monomodular T1PKS biosynthetic gene clusters (BGCs) were experimentally confirmed to be iteratively acting, synthesizing diverse branched/nonbranched linear intermediates, and two of them produced bioactive allenic polyketides and citreodiols as end products, respectively. This study indicates the huge potential of iterative T1PKS BGCs from streptomycetes in the discovery of novel polyketides.

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Iterative polyketide biosynthesis by modular polyketide synthases in bacteria.

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The structural organization of substrate loading in iterative polyketide synthases.

Project description:Polyketide synthases (PKSs) are microbial multienzymes for the biosynthesis of biologically potent secondary metabolites. Polyketide production is initiated by the loading of a starter unit onto an integral acyl carrier protein (ACP) and its subsequent transfer to the ketosynthase (KS). Initial substrate loading is achieved either by multidomain loading modules or by the integration of designated loading domains, such as starter unit acyltransferases (SAT), whose structural integration into PKS remains unresolved. A crystal structure of the loading/condensing region of the nonreducing PKS CTB1 demonstrates the ordered insertion of a pseudodimeric SAT into the condensing region, which is aided by the SAT-KS linker. Cryo-electron microscopy of the post-loading state trapped by mechanism-based crosslinking of ACP to KS reveals asymmetry across the CTB1 loading/-condensing region, in accord with preferential 1:2 binding stoichiometry. These results are critical for re-engineering the loading step in polyketide biosynthesis and support functional relevance of asymmetric conformations of PKSs.

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Short-chain ketone production by engineered polyketide synthases in Streptomyces albus.

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Correction for Wang et al., "Porcine MKRN1 Modulates the Replication and Pathogenesis of Porcine Circovirus Type 2 by Inducing Capsid Protein Ubiquitination and Degradation".

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Correction: Wang, F., et al. Effect of Low-Frequency Electromagnetic Casting on Micro-Structure and Macro-Segregation of 5A90 Alloy Ingots. Materials 2020, 13, 2720.

Project description:In the original article [...].

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