Barber_2013_J.Biol.Chem_288_12500

Reference

Title : 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 - Barber_2013_J.Biol.Chem_288_12500
Author(s) : Barber CJ , Pujara PT , Reed DW , Chiwocha S , Zhang H , Covello PS
Ref : Journal of Biological Chemistry , 288 :12500 , 2013
Abstract :

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.

PubMedSearch : Barber_2013_J.Biol.Chem_288_12500
PubMedID: 23486480
Gene_locus related to this paper: 9cary-r4p353

Related information

Gene_locus 9cary-r4p353

Citations formats

Barber CJ, Pujara PT, Reed DW, Chiwocha S, Zhang H, Covello PS (2013)
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
Journal of Biological Chemistry 288 :12500

Barber CJ, Pujara PT, Reed DW, Chiwocha S, Zhang H, Covello PS (2013)
Journal of Biological Chemistry 288 :12500