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ProteomicsDifferential prolyl hydroxylation by six Physcomitrella prolyl-4 hydroxylases
The hydroxylation of proline residues to 4-trans-hydroxyproline (Hyp) is a common post-translational protein modification in plants, mediated by prolyl 4-hydroxylases (P4Hs). Hyps predominantly occur in a group of cell wall proteins, the Hydroxyproline-rich glycoproteins (HRGPs), where they are freq...
ORGANISM(S): Physcomitrella patens subsp. patens (Moss) 
2024-08-10 | PXD051497 | Pride
O-glycosylation Posttranslational protein modification Erythropoietin Prolyl-hydroxylation Biopharmaceutical Plant-made pharmaceutical 
ProteomicsUnexpected arabinosylation after humanization of plant protein N-glycosylation
As biopharmaceuticals, recombinant proteins have become indispensable tools in medicine. An increasing demand, not only in quantity but also in diversity, drives the constant development and improvement of production platforms. The N-glycosylation pattern on biopharmaceuticals plays important roles ...
ORGANISM(S): Physcomitrella 
2022-04-04 | PXD030443 | Pride
Physcomitrella (physcomitrium patens) Plant-made recombinant biopharmaceuticals 4-galactosylation Glyco-optimization N-glycan humanization Glyco-engineering Plant-made pharmaceuticals Β1 N-glycan pentosylation 
ProteomicsIdentification of N-terminally arginylated proteins from the moss Physcomitrella patens
Protein arginylation is a post-translational modification at the N-terminus of proteins and is crucial for viability and physiology in higher eukaryotes. The lack of arginylation causes severe developmental defects in plants and embryo lethality in Drosophila and in mice. Although several studies in...
ORGANISM(S): Physcomitrella patens subsp. patens (Moss) 
2016-04-21 | PXD003232 | Pride
N-end rule pathway Arginylation Physcomitrella patens 
ProteomicsExpression of a human cDNA in moss results in spliced mRNAs and fragmentary protein isoforms
Production of biopharmaceuticals relies on the expression of mammalian cDNAs in host organisms. Here we show that the expression of a human cDNA in the moss Physcomitrium patens generates the expected full-length and four additional transcripts due to unexpected splicing. This mRNA splicing results ...
ORGANISM(S): Physcomitrella patens subsp. patens (Moss) 
2022-01-10 | PXD026651 | Pride
Aberrant mrna-splicing Heterologous expression systems Physcomitrium patens Blood coagulation factor ix 
ProteomicsA snapshot of the Physcomitrella N-terminome reveals N-terminal methylation of organellar proteins
Post- or co-translational modifications of protein N-termini influence their half-life and mediate protein sorting to organelles via cleavable N-terminal sequences that are recognized by the respective translocation machinery. In the present study, we provide an overview on the current modification ...
ORGANISM(S): Physcomitrella patens subsp. patens (Moss) 
2025-05-07 | PXD052824 | Pride
Physcomitrium Methylation Moss Mass spectrometry N-terminus 
ProteomicsThe host cell proteome of Physcomitrella patens
Host cell proteins are inevitable contaminants of biopharmaceuticals. Here, we performed detailed analyses of the host cell proteome of moss (Physcomitrella patens) bioreactor supernatants using mass spectrometry and subsequent bioinformatics analysis. Distinguishing between the apparent secretome a...
ORGANISM(S): Physcomitrella patens subsp. patens (Moss) 
2018-09-19 | PXD009517 | Pride
Bioreactor Physcomitrella patens Host cell proteome 
ProteomicsA deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in aging in Physcomitrella and Arabidopsis
Protein oxidation results from the reaction of amino-acid side chains with reactive oxygen species (ROS) and is mostly irreversible. In non-photosynthetic tissues, mitochondria are a main source of ROS, whereas plastids are the major source in photosynthetic tissues. Oxidized proteins suffer from de...
ORGANISM(S): Physcomitrella patens subsp. patens (Moss) 
2023-03-11 | PXD033854 | Pride
Arabidopsis Ageing Physcomitrella Ros Physcomitrium Protein oxidation 
ProteomicsA deeply cA deeply conserved protease, acylamino acid-releasing enzyme (AARE), acts in ageing in Physcomitrella and Arabidopsis
Reactive oxygen species (ROS) are constant by-products of aerobic life. In excess, ROS lead to cytotoxic protein aggregates, which are a hallmark of ageing in animals and linked to age-related pathologies in humans. Acylamino acid-releasing enzymes (AARE) are bifunctional serine proteases, acting on...
ORGANISM(S): Physcomitrella 
2023-03-11 | PXD038742 | Pride
Plant ageing Ros Aging Physcomitrium Protein oxidation 
ProteomicsProduction of recombinant human collagen in Physcomitrella
A hydrophilic region encompassing 334 amino acids from human type III collagen was produced in Physcomitrella bioreactors and analyzed with respect to prolyl-hydroxylation.
ORGANISM(S): Physcomitrella patens subsp. patens (Moss) 
2026-02-09 | PXD071319 | Pride
Col3a1 Moss bioreactor Physcomitrella Prolyl hydroxylated collagen 
ProteomicsProduction of recombinant human type III collagen in Physcomitrella
We produced a 30 kDa His-tagged human collagen polypeptide in Physcomitrella moss plants.
ORGANISM(S): Physcomitrella patens subsp. patens (Moss) 
2026-02-09 | PXD071359 | Pride
Collagen Physcomitrella 
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