Abstract 1506 Native top-down mass spectrometry analysis of nucleosomes and histone proteoforms
Nucleosomes are nucleoprotein complexes that act as the core architecture of chromatin and contain 4 distinct histone subunits: H2A, H2B, H3, and H4. Histones contain complex post-translational modifications (PTMs) to produce specific histone proteoforms and these proteoforms are biomarkers of epigenetic deregulation linked to cancers including pediatric glioblastoma. Studying histone proteoforms in the context of the whole nucleosome provides a read out of the proteoforms from a diverse population of nucleosomes while reducing identification of non-specific histone contaminants in nucleosome pull-downs.
Authors
- Matthew R. Marunde (ORCID: https://orcid.org/0009-0007-5934-7200)
- Michael-Christopher Keogh
- Philip D. Compton (ORCID: https://orcid.org/0000-0001-5212-7175)
- Neil L. Kelleher (ORCID: https://orcid.org/0000-0002-8815-3372)
- Jared O. Kafader (ORCID: https://orcid.org/0000-0002-5359-264X)
- Rafael D. Melani (ORCID: https://orcid.org/0000-0002-0349-235X)
- Michael W. Senko (ORCID: https://orcid.org/0009-0000-5040-5776)
- Nickolas P. Fisher (ORCID: https://orcid.org/0000-0002-8574-7503)
- Alexander Lee (ORCID: https://orcid.org/0000-0001-6237-5498)
Institutions
- Northwestern University (PH)
- Northwestern College - Iowa (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109243
- Primary Topic
- RNA modifications and cancer
- Type
- article
- Field-Weighted Citation Impact
- 0.00