SMC Affiliated Work
1
Status
Faculty
School
School of Science
Department
Biology
Document Type
Article
Publication Date
2017
Publication / Conference / Sponsorship
Journal of Proteome Research
Description/Abstract
The unicellular microalga Chlamydomonas reinhardtii has played an instrumental role in the development of many new fields (bioproducts, biofuels, etc.) as well as the advancement of basic science (photosynthetic apparati, flagellar function, etc.). Chlamydomonas' versatility ultimately derives from the genes encoded in its genome and the way that the expression of these genes is regulated, which is largely influenced by a family of DNA binding proteins called histones. We characterize C. reinhardtii core histones, both variants and their post-translational modifications, by chromatographic separation, followed by top-down mass spectrometry (TDMS). Because TDMS has not been previously used to study Chlamydomonas proteins, we show rampant artifactual protein oxidation using established nuclei purification and histone extraction methods. After addressing oxidation, both histones H3 and H4 are found to each have a single polypeptide sequence that is minimally acetylated and methylated. Surprisingly, we uncover a novel monomethylation at lysine 79 on histone H4 present on all observed molecules. Histone H2B and H2A are found to have two and three variants, respectively, and both are minimally modified. This study provides an updated assessment of the core histone proteins in the green alga C. reinhardtii by top-down mass spectrometry and lays the foundation for further investigation of these essential proteins.
Keywords
epigenetics, histones, microalgae, post-translational modifications, top-down mass spectrometry
Scholarly
yes
DOI
10.1021/acs.jproteome.7b00780
Disciplines
Biology
Rights
Open Access. Author Manuscript. Author permission to post in Saint Mary’s Digital Commons
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
Original Citation
Khan, A, Eikani, C. K., Khan, H., Iavarone, A. T., and Pesavento, J. J. “Characterization of Chlamydomonas reinhardtii core histones by top-down mass spectrometry reveals unique algae-specific variants and post-translational modifications.” Journal of Proteome Research. 2017.
Repository Citation
Khan, Aliyya; Eikani, Carlo; Khan, Hana; Iavarone, Anthony; and Pesavento, James. Characterization of Chlamydomonas reinhardtii Core Histones by Top-Down Mass Spectrometry Reveals Unique Algae-Specific Variants and Post-Translational Modifications (2017). Journal of Proteome Research. 10.1021/acs.jproteome.7b00780 [article]. https://digitalcommons.stmarys-ca.edu/school-science-faculty-works/168
Link to Published Version
https://doi.org/10.1021/acs.jproteome.7b00780
