Journal article
Proteome-wide analysis reveals widespread lysine acetylation of major protein complexes in the malaria parasite
SA Cobbold, JM Santos, A Ochoa, DH Perlman, M Llinas
Scientific Reports | NATURE PORTFOLIO | Published : 2016
DOI: 10.1038/srep19722
Abstract
Lysine acetylation is a ubiquitous post-translational modification in many organisms including the malaria parasite Plasmodium falciparum, yet the full extent of acetylation across the parasite proteome remains unresolved. Moreover, the functional significance of acetylation or how specific acetyl-lysine sites are regulated is largely unknown. Here we report a seven-fold expansion of the known parasite 'acetylome', characterizing 2,876 acetylation sites on 1,146 proteins. We observe that lysine acetylation targets a diverse range of protein complexes and is particularly enriched within the Apicomplexan AP2 (ApiAP2) DNA-binding protein family. Using quantitative proteomics we determined that ..
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Awarded by National Institutes of Health
Funding Acknowledgements
We thank Henry Shwe at the Collaborative Proteomics and Mass Spectrometry Center for assisting with protein/peptide sample processing, Manuela Carrasquilla for assistance with the acetate treatment experiment, Heather Painter for her thoughtful comments throughout the project and Scott Lindner for his valuable comments on the manuscript. We thank Manoj Duraisingh for providing Sir2-13 (aka Sir2a) and Sir2-14 (aka Sir2b) knockout lines. This work was funded through generous support from the Burroughs Welcome Fund, an NIH Director's New Innovators award (1DP2OD001315-01), the Center for Quantitative Biology (P50 GM071508), and startup funding from the Pennsylvania State University. JMS was supported by an EMBO long-term fellowship (633-2011) and a Bourses pour chercheuses et chercheurs debutants from the Swiss National Foundation (GEP3-13613).