Proteoforms expand the world of microproteins and short open reading frame-encoded peptides

Microproteins and short open reading frame-encoded peptides (SEPs) can, like all proteins, carry numerous posttranslational modifications. Together with posttranscriptional processes, this leads to a high number of possible distinct protein molecules, the proteoforms, out of a limited number of gene...

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Published in:iScience 2023-02, Vol.26 (2), p.106069-106069, Article 106069
Main Authors: Cassidy, Liam, Kaulich, Philipp T., Tholey, Andreas
Format: Article
Language:English
Subjects:
Biochemistry
Molecular biology
Molecular mechanism of gene regulation
Proteomics
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Summary:Microproteins and short open reading frame-encoded peptides (SEPs) can, like all proteins, carry numerous posttranslational modifications. Together with posttranscriptional processes, this leads to a high number of possible distinct protein molecules, the proteoforms, out of a limited number of genes. The identification, quantification, and molecular characterization of proteoforms possess special challenges to established, mainly bottom-up proteomics (BUP) based analytical approaches. While BUP methods are powerful, proteins have to be inferred rather than directly identified, which hampers the detection of proteoforms. An alternative approach is top-down proteomics (TDP) which allows to identify intact proteoforms. This perspective article provides a brief overview of modified microproteins and SEPs, introduces the proteoform terminology, and compares present BUP and TDP workflows highlighting their major advantages and caveats. Necessary future developments in TDP to fully accentuate its potential for proteoform-centric analytics of microproteins and SEPs will be discussed. [Display omitted] Biochemistry; Molecular biology; Molecular mechanism of gene regulation; Proteomics
ISSN:2589-0042
2589-0042
DOI:10.1016/j.isci.2023.106069