The Two-step biosynthesis of cyclic peptides from linear precursors in a member of the plant family Caryophyllaceae involves cyclization by a Serine Protease-like enzyme

Alternative titleA serine protease-like enzyme involved in cyclic peptide biosynthesis in the plant family Caryophyllaceae
Caryophyllaceae cyclic peptide biosynthesis
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DOIResolve DOI: http://doi.org/10.1074/jbc.M112.437947
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TypeArticle
Journal titleJournal of Biological Chemistry
ISSN0021-9258
1083-351X
Volume288
Issue18
Pages1250012510; # of pages: 11
SubjectPeptidases; peptide biosythesis; plant biochemsitry; plant molecular biology; protease; Caryophyllaceae; Saponaria vaccaria; cyclic peptide; peptide cyclase; orbitide
AbstractBackground: In the Caryophyllaceae, cyclic peptides (CP) are biosynthesized from linear precursors via an unknown pathway. Results: Two protease-like enzymes are involved in precursor processing. Conclusion: A serine protease-like enzyme was recruited for the cyclization step in CP biosynthesis. Significance: This represents a very significant advance in our understanding of the mode and evolution of CP biosynthesis in plants. Caryophyllaceae-type cyclic peptides (CPs) of 5–12 proteinogenic amino acids occur in 10 plant families. In Saponaria vaccaria (Caryophyllaceae), they have been shown to be formed from linear peptide precursors derived from ribosomal translation. There is also evidence for such precursors in other members of the Caryophyllaceae, Rutaceae, and Linaceae families. The biosynthesis of CP in the developing seeds of S. vaccaria was investigated with respect to the enzymes involved in precursor processing. Through biochemical assays with seed extracts and synthetic peptides, an enzyme named oligopeptidase 1 (OLP1) was found that catalyzes the cleavage of intermediates at the N terminus of the incipient CP. A second enzyme, peptide cyclase 1 (PCY1), which was separated chromatographically from OLP1, was found to act on the product of OLP1, giving rise to a cyclic peptide and concomitant removal of a C-terminal flanking sequence. PCY1 was partially purified, and using the methods of proteomics, a full-length cDNA clone encoding an enzyme matching the properties of PCY1 was obtained. The substrate specificity of purified recombinant PCY1, believed to be the first cloned plant enzyme whose function is peptide cyclization, was tested with synthetic peptides. The results are discussed in the light of CP biosynthetic systems of other organisms.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; Aquatic and Crop Resource Development; NRC Plant Biotechnology Institute
Peer reviewedYes
NRC number55422
NPARC number21268490
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Record identifierfaa9a231-9564-4805-8773-fdee91611fdc
Record created2013-08-15
Record modified2016-05-09
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