A snapshot of the Physcomitrella N-terminome reveals N-terminal methylation of organellar proteins
Open accessPublished version of a preprint
Abstract
Key message: Analysis of the N-terminome of Physcomitrella reveals N-terminal monomethylation of nuclear-encoded, mitochondria-localized proteins. Post- or co-translational N-terminal modifications of proteins influence their half-life as well as mediating protein sorting to organelles via cleavable N-terminal sequences that are recognized by the respective translocation machinery. Here, we provide an overview on the current modification state of the N-termini of over 4500 proteins from the model moss Physcomitrella ( Physcomitrium patens ) using a compilation of 24 N-terminomics datasets. Our data reveal distinct proteoforms and modification states and confirm predicted targeting peptide cleavage sites of 1,144 proteins localized to plastids and the thylakoid lumen, to mitochondria, and to the secretory pathway. In addition, we uncover extended N-terminal methylation of mitochondrial proteins. Moreover, we identified PpNTM1 ( P. patens alpha N-terminal protein methyltransferase 1) as a candidate for protein methylation in plastids, mitochondria, and the cytosol. These data can now be used to optimize computational targeting predictors, for customized protein fusions and their targeted localization in biotechnology, and offer novel insights into potential dual targeting of proteins. Graphical abstract:
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- Authors
- Hoernstein, S. N. W., Schlosser, A., Fiedler, K., van Gessel, N., Igloi, G. L., Lang, D., & Reski, R.
- Affiliations
- University of Freiburg (DE)
- ORCID
- Venue
- Plant Cell Reports
- Published
- 2024-10
- Volume
- 43
- Issue
- 10
- Pages
- 250-250
- ISSN
- 0721-7714 (ISSN-L)
- 1432-203X
- PMC
- PMC11450134
- OpenAlex
- W4403104721
- Cited by
- 5
- References
- 7
- Citations by year
- 2025: 5
- FWCI
- 0.62
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Plant Cell Reports (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Online Publication Service of Würzburg University (Würzburg University) (submittedVersion, cc-by)
- FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (EXC-2189, IG9/8)
- Albert-Ludwigs-Universität Freiburg im Breisgau
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Keywords
- N-terminome, N-terminal methylation, Physcomitrella patens, bryophytes, mitochondrial proteins, plastid proteins, thylakoid lumen, secretory pathway, dual targeting, protein localization, proteoforms, N-terminomics
- MeSH terms
- Methylation, Mitochondria, Plant Proteins, Protein Processing, Post-Translational, Organelles, Plastids, Bryopsida, Protein Transport, Mitochondrial Proteins, Proteomics
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