Evolutionary origins of a bioactive peptide buried within preproalbumin

Elliott, Alysha G., Delay, Christina, Liu, Huanle, Phua, Zaiyang, Rosengren, K. Johan, Benfield, Aurelie H., Panero, Jose L., Colgrave, Michelle L., Jayasena, Achala S., Dunse, Kerry M., Anderson, Marilyn A., Schilling, Edward E., Ortiz-Barrientos, Daniel, Craik, David J. and Mylne, Joshua S. (2014) Evolutionary origins of a bioactive peptide buried within preproalbumin. The Plant Cell, 26 3: 981-995. doi:10.1105/tpc.114.123620


Author Elliott, Alysha G.
Delay, Christina
Liu, Huanle
Phua, Zaiyang
Rosengren, K. Johan
Benfield, Aurelie H.
Panero, Jose L.
Colgrave, Michelle L.
Jayasena, Achala S.
Dunse, Kerry M.
Anderson, Marilyn A.
Schilling, Edward E.
Ortiz-Barrientos, Daniel
Craik, David J.
Mylne, Joshua S.
Title Evolutionary origins of a bioactive peptide buried within preproalbumin
Journal name The Plant Cell   Check publisher's open access policy
ISSN 1040-4651
1532-298X
Publication date 2014-03
Year available 2014
Sub-type Article (original research)
DOI 10.1105/tpc.114.123620
Open Access Status
Volume 26
Issue 3
Start page 981
End page 995
Total pages 15
Place of publication Rockville, MD, United States
Publisher American Society of Plant Biologists
Collection year 2015
Language eng
Formatted abstract
The de novo evolution of proteins is now considered a frequented route for biological innovation, but the genetic and biochemical processes that lead to each newly created protein are often poorly documented. The common sunflower (Helianthus annuus) contains the unusual gene PawS1 (Preproalbumin with SFTI-1) that encodes a precursor for seed storage albumin; however, in a region usually discarded during albumin maturation, its sequence is matured into SFTI-1, a protease-inhibiting cyclic peptide with a motif homologous to unrelated inhibitors from legumes, cereals, and frogs. To understand how PawS1 acquired this additional peptide with novel biochemical functionality, we cloned PawS1 genes and showed that this dual destiny is over 18 million years old. This new family of mostly backbone-cyclic peptides is structurally diverse, but the protease-inhibitory motif was restricted to peptides from sunflower and close relatives from its subtribe. We describe a widely distributed, potential evolutionary intermediate PawS-Like1 (PawL1), which is matured into storage albumin, but makes no stable peptide despite possessing residues essential for processing and cyclization from within PawS1. Using sequences we cloned, we retrodict the likely stepwise creation of PawS1’s additional destiny within a simple albumin precursor. We propose that relaxed selection enabled SFTI-1 to evolve its inhibitor function by converging upon a successful sequence and structure.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
School of Biological Sciences Publications
Institute for Molecular Bioscience - Publications
 
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Citation counts: TR Web of Science Citation Count  Cited 9 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 9 times in Scopus Article | Citations
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Created: Thu, 03 Apr 2014, 14:18:02 EST by Susan Allen on behalf of Institute for Molecular Bioscience