Cyclic peptides arising by evolutionary parallelism via asparaginyl-endopeptidase–mediated biosynthesis

Mylne, Joshua S., Chan, Lai Yue, Chanson, Aurelie H., Daly, Norelle L., Schaefer, Hanno, Bailey, Timothy L., Nguyencong, Philip, Cascales, Laura and Craik, David J. (2012) Cyclic peptides arising by evolutionary parallelism via asparaginyl-endopeptidase–mediated biosynthesis. Plant Cell, 24 7: 2765-2778. doi:10.1105/tpc.112.099085


Author Mylne, Joshua S.
Chan, Lai Yue
Chanson, Aurelie H.
Daly, Norelle L.
Schaefer, Hanno
Bailey, Timothy L.
Nguyencong, Philip
Cascales, Laura
Craik, David J.
Title Cyclic peptides arising by evolutionary parallelism via asparaginyl-endopeptidase–mediated biosynthesis
Journal name Plant Cell   Check publisher's open access policy
ISSN 1040-4651
1532-298X
Publication date 2012-07
Sub-type Article (original research)
DOI 10.1105/tpc.112.099085
Volume 24
Issue 7
Start page 2765
End page 2778
Total pages 14
Place of publication Rockville, MD, United States
Publisher American Society of Plant Biologists
Collection year 2013
Language eng
Formatted abstract
The cyclic miniprotein Momordica cochinchinensis Trypsin Inhibitor II (MCoTI-II) (34 amino acids) is a potent trypsin inhibitor (TI) and a favored scaffold for drug design. We have cloned the corresponding genes and determined that each precursor protein contains a tandem series of cyclic TIs terminating with the more commonly known, and potentially ancestral, acyclic TI. Expression of the precursor protein in Arabidopsis thaliana showed that production of the cyclic TIs, but not the terminal acyclic TI, depends on asparaginyl endopeptidase (AEP) for maturation. The nature of their repetitive sequences and the almost identical structures of emerging TIs suggest these cyclic peptides evolved by internal gene amplification associated with recruitment of AEP for processing between domain repeats. This is the third example of similar AEP-mediated processing of a class of cyclic peptides from unrelated precursor proteins in phylogenetically distant plant families. This suggests that production of cyclic peptides in angiosperms has evolved in parallel using AEP as a constraining evolutionary channel. We believe this is evolutionary evidence that, in addition to its known roles in proteolysis, AEP is especially suited to performing protein cyclization.
Keyword Vacuolar processing enzyme
Cystine knot motif
Inhibitor MCoTI-II
Circular proteins
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2013 Collection
Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 46 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 46 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Fri, 03 Aug 2012, 09:25:16 EST by Susan Allen on behalf of Institute for Molecular Bioscience