An interstitial peptide is readily processed from within seed proteins
| Autor: | Benjamin Pouvreau, Monika W. Murcha, Joshua S. Mylne, Ricarda Fenske, Aneta Ivanova |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Proteomics
0106 biological sciences 0301 basic medicine Transgene Arabidopsis Sequence (biology) Peptide Plant Science Biology Peptides Cyclic Polymerase Chain Reaction 01 natural sciences 03 medical and health sciences chemistry.chemical_compound Genetics Protein biosynthesis Amino Acid Sequence Gene Plant Proteins chemistry.chemical_classification Albumin General Medicine Plants Genetically Modified Endopeptidase 030104 developmental biology Biochemistry chemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Seeds Helianthus Agronomy and Crop Science DNA 010606 plant biology & botany |
| Zdroj: | Plant Science. 285:175-183 |
| ISSN: | 0168-9452 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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