Evidence map›Paper›PMID 24681618›Full record

ArticleThe Plant cell2014

Evolutionary origins of a bioactive peptide buried within Preproalbumin.

Alysha G Elliott, Christina Delay, Huanle Liu, Zaiyang Phua, K Johan Rosengren, Aurélie H Benfield, Jose L Panero, Michelle L Colgrave, Achala S Jayasena, Kerry M Dunse and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Rational design of glycosaminoglycan binding cyclic peptides using cPEPmatch.Computational and structural biotechnology journal · 2024
    Article
  3. Review
  4. Mechanisms of protein evolution.Protein science : a publication of the Protein Society · 2022
    Review
  5. Article
  6. Plant derived cyclic peptides.Biochemical Society transactions · 2021
    Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. A tripartite approach identifies the major sunflower seed albumins.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2016
    Article
  17. Review
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors at 6 institutions in 2 countries.

Alysha G ElliottThe University of Queensland, Institute for Molecular Bioscience, Brisbane 4072, Australia.
Christina Delay
Huanle Liu
Zaiyang Phua
K Johan Rosengren
Aurélie H Benfield
Jose L Panero
Michelle L Colgrave
Achala S Jayasena
Kerry M Dunse
Marilyn A Anderson
Edward E Schilling
Daniel Ortiz-Barrientos
David J Craik
Joshua S Mylne
University of Queensland · AULa Trobe University · AUUniversity of Western Australia · AUCommonwealth Scientific and Industrial Research Organisation · AUThe University of Texas at Austin · USUniversity of Tennessee at Knoxville · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Evolution, MolecularAmino Acid SequenceMolecular Sequence DataPeptidesPhylogenyPrealbuminProtein PrecursorsSeedsSequence Homology, Amino AcidPeptidesPrealbuminpreproalbuminProtein Precursors

Identifiers

PMID24681618
PMCPMC4001405
OpenAlexW2133891072

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.