An interstitial peptide is readily processed from within seed proteins

Research output: Contribution to journalArticle

Abstract

The importance of de novo protein evolution is apparent, but most examples are de novo coding transcripts evolving from silent or non-coding DNA. The peptide macrocycle SunFlower Trypsin Inhibitor 1 (SFTI-1) evolved over 45 million years from genetic expansion within the N-terminal ‘discarded’ region of an ancestral seed albumin precursor. SFTI-1 and its adjacent albumin are both processed into separate, mature forms by asparaginyl endopeptidase (AEP). Here to determine whether the evolution of SFTI-1 in a latent region of its precursor was critical, we used a transgene approach in A. thaliana analysed by peptide mass spectrometry and RT-qPCR. SFTI could emerge from alternative locations within preproalbumin as well as emerge with precision from unrelated seed proteins via AEP-processing. SFTI production was possible with the adjacent albumin, but peptide levels dropped greatly without the albumin. The ability for SFTI to be processed from multiple sequence contexts and different proteins suggests that to make peptide, it was not crucial for the genetic expansion that gave rise to SFTI and its family to be within a latent protein region. Interstitial peptides, evolving like SFTI within existing proteins, might be more widespread and as a mechanism, SFTI exemplifies a stable, new, functional peptide that did not need a new gene to evolve de novo.

Original languageEnglish
Pages (from-to)175-183
Number of pages9
JournalPlant Science
Volume285
DOIs
Publication statusPublished - 1 Aug 2019

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Seeds
asparaginylendopeptidase
peptides
Peptides
albumins
Albumins
trypsin inhibitors
seeds
Helianthus annuus
Proteins
proteins
proteinases
intergenic DNA
Transgenes
transgenes
Mass Spectrometry
mass spectrometry
DNA
Genes
sunflower SFTI-1 peptide

Cite this

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title = "An interstitial peptide is readily processed from within seed proteins",
abstract = "The importance of de novo protein evolution is apparent, but most examples are de novo coding transcripts evolving from silent or non-coding DNA. The peptide macrocycle SunFlower Trypsin Inhibitor 1 (SFTI-1) evolved over 45 million years from genetic expansion within the N-terminal ‘discarded’ region of an ancestral seed albumin precursor. SFTI-1 and its adjacent albumin are both processed into separate, mature forms by asparaginyl endopeptidase (AEP). Here to determine whether the evolution of SFTI-1 in a latent region of its precursor was critical, we used a transgene approach in A. thaliana analysed by peptide mass spectrometry and RT-qPCR. SFTI could emerge from alternative locations within preproalbumin as well as emerge with precision from unrelated seed proteins via AEP-processing. SFTI production was possible with the adjacent albumin, but peptide levels dropped greatly without the albumin. The ability for SFTI to be processed from multiple sequence contexts and different proteins suggests that to make peptide, it was not crucial for the genetic expansion that gave rise to SFTI and its family to be within a latent protein region. Interstitial peptides, evolving like SFTI within existing proteins, might be more widespread and as a mechanism, SFTI exemplifies a stable, new, functional peptide that did not need a new gene to evolve de novo.",
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An interstitial peptide is readily processed from within seed proteins. / Pouvreau, Benjamin; Fenske, Ricarda; Ivanova, Aneta; Murcha, Monika W.; Mylne, Joshua S.

In: Plant Science, Vol. 285, 01.08.2019, p. 175-183.

Research output: Contribution to journalArticle

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AU - Ivanova, Aneta

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