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

From National Research Council Canada

Alternative title	A serine protease-like enzyme involved in cyclic peptide biosynthesis in the plant family Caryophyllaceae Caryophyllaceae cyclic peptide biosynthesis
Download	View accepted manuscript: 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 (PDF, 612 KiB)
DOI	Resolve DOI: https://doi.org/10.1074/jbc.M112.437947
Author	Search for: Barber, Carla J. S.¹; Search for: Pujara, Pareshkumar T.¹; Search for: Reed, Darwin W.¹; Search for: Chiwocha, Shiela²; Search for: Zhang, Haixia¹; Search for: Covello, Patrick S.¹
Affiliation	National Research Council of Canada. Aquatic and Crop Resource Development National Research Council of Canada. NRC Plant Biotechnology Institute
Format	Text, Article
Subject	peptidases; peptide biosythesis; plant biochemsitry; plant molecular biology; protease; Caryophyllaceae; Saponaria vaccaria; cyclic peptide; peptide cyclase; orbitide
Abstract	Background: 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	2013-05-03
Publisher	American Society for Biochemistry and Molecular Biology
In	The Journal of Biological Chemistry 288, no. 18: 12500–12510.
Language	English
Peer reviewed	Yes
NRC number	NRCC 55422
NPARC number	21268490
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Record identifier	faa9a231-9564-4805-8773-fdee91611fdc
Record created	2013-08-15
Record modified	2020-06-04

Date modified:: 2024-10-21