The Discovery of New Cyanobactins from Cyanothece PCC 7425 Defines a New Signature for Processing of Patellamides
Cyanobactins, including patellamides, are a group of cyanobacterial post‐translationally modified ribosomal cyclic peptides. The final product should in theory be predictable from the sequence of the precursor peptide and the associated tailoring enzymes. Understanding the mechanism and recognition...
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Published in | Chembiochem : a European journal of chemical biology Vol. 13; no. 18; pp. 2683 - 2689 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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Weinheim
WILEY-VCH Verlag
21.12.2012
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Abstract | Cyanobactins, including patellamides, are a group of cyanobacterial post‐translationally modified ribosomal cyclic peptides. The final product should in theory be predictable from the sequence of the precursor peptide and the associated tailoring enzymes. Understanding the mechanism and recognition requirements of these enzymes will allow their rational engineering. We have identified three new cyanobactins from a Cyanothece PCC 7425 culture subjected to a heat shock. One of these compounds revealed a novel signature signal for ThcA, the subtilisin‐like serine protease that is homologous to the patellamide protease PatA. The crystal structure of the latter and modelling studies allow rationalisation of the recognition determinants for both enzymes, consistent with the ribosomal biosynthetic origin of the new compounds.
Follow the signal: The discovery of new cyanobactins from Cyanothece PCC 7425 cultured under stressful conditions revealed a novel signature signal for its subtilisin protease that is homologous to the patellamide protease PatA. The crystal structure of the latter and modelling studies have provided a molecular rationalisation for the enzyme specificity, a step which will enhance harnessing the full capacity of these biosynthetic enzymes. |
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AbstractList | Cyanobactins, including patellamides, are a group of cyanobacterial post-translationally modified ribosomal cyclic peptides. The final product should in theory be predictable from the sequence of the precursor peptide and the associated tailoring enzymes. Understanding the mechanism and recognition requirements of these enzymes will allow their rational engineering. We have identified three new cyanobactins from a Cyanothece PCC 7425 culture subjected to a heat shock. One of these compounds revealed a novel signature signal for ThcA, the subtilisin-like serine protease that is homologous to the patellamide protease PatA. The crystal structure of the latter and modelling studies allow rationalisation of the recognition determinants for both enzymes, consistent with the ribosomal biosynthetic origin of the new compounds. [PUBLICATION ABSTRACT] Cyanobactins, including patellamides, are a group of cyanobacterial post-translationally modified ribosomal cyclic peptides. The final product should in theory be predictable from the sequence of the precursor peptide and the associated tailoring enzymes. Understanding the mechanism and recognition requirements of these enzymes will allow their rational engineering. We have identified three new cyanobactins from a Cyanothece PCC 7425 culture subjected to a heat shock. One of these compounds revealed a novel signature signal for ThcA, the subtilisin-like serine protease that is homologous to the patellamide protease PatA. The crystal structure of the latter and modelling studies allow rationalisation of the recognition determinants for both enzymes, consistent with the ribosomal biosynthetic origin of the new compounds. Cyanobactins, including patellamides, are a group of cyanobacterial post‐translationally modified ribosomal cyclic peptides. The final product should in theory be predictable from the sequence of the precursor peptide and the associated tailoring enzymes. Understanding the mechanism and recognition requirements of these enzymes will allow their rational engineering. We have identified three new cyanobactins from a Cyanothece PCC 7425 culture subjected to a heat shock. One of these compounds revealed a novel signature signal for ThcA, the subtilisin‐like serine protease that is homologous to the patellamide protease PatA. The crystal structure of the latter and modelling studies allow rationalisation of the recognition determinants for both enzymes, consistent with the ribosomal biosynthetic origin of the new compounds. Cyanobactins, including patellamides, are a group of cyanobacterial post‐translationally modified ribosomal cyclic peptides. The final product should in theory be predictable from the sequence of the precursor peptide and the associated tailoring enzymes. Understanding the mechanism and recognition requirements of these enzymes will allow their rational engineering. We have identified three new cyanobactins from a Cyanothece PCC 7425 culture subjected to a heat shock. One of these compounds revealed a novel signature signal for ThcA, the subtilisin‐like serine protease that is homologous to the patellamide protease PatA. The crystal structure of the latter and modelling studies allow rationalisation of the recognition determinants for both enzymes, consistent with the ribosomal biosynthetic origin of the new compounds. Follow the signal: The discovery of new cyanobactins from Cyanothece PCC 7425 cultured under stressful conditions revealed a novel signature signal for its subtilisin protease that is homologous to the patellamide protease PatA. The crystal structure of the latter and modelling studies have provided a molecular rationalisation for the enzyme specificity, a step which will enhance harnessing the full capacity of these biosynthetic enzymes. |
Author | Raab, Andrea Smith, Margaret C. M. Vendome, Jeremie Zollman, David Houssen, Wael E. Naismith, James H. Jaspars, Marcel Koehnke, Jesko |
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Keywords | subtilisin proteases SUBTILISIN ribosomal peptides cyanobactins biosynthetic engineering PEPTIDE MARINE NATURAL-PRODUCTS REFINEMENT natural products GENE-CLUSTER BIOSYNTHESIS SEQUENCE EXPRESSION MACROCYCLIZATION LISSOCLINUM-PATELLA |
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Snippet | Cyanobactins, including patellamides, are a group of cyanobacterial post‐translationally modified ribosomal cyclic peptides. The final product should in theory... Cyanobactins, including patellamides, are a group of cyanobacterial post-translationally modified ribosomal cyclic peptides. The final product should in theory... |
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SubjectTerms | Amino Acid Sequence Biochemistry & Molecular Biology biosynthetic engineering Chemistry, Medicinal Crystal structure cyanobactins Cyanothece - metabolism Life Sciences & Biomedicine Models, Molecular Molecular Sequence Data natural products Peptides, Cyclic - chemistry Peptides, Cyclic - metabolism Pharmacology & Pharmacy Protein Processing, Post-Translational Protein Structure, Tertiary ribosomal peptides Science & Technology Serine Proteases - chemistry Serine Proteases - metabolism subtilisin proteases |
Title | The Discovery of New Cyanobactins from Cyanothece PCC 7425 Defines a New Signature for Processing of Patellamides |
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