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Comprehensive Histone Phosphorylation Analysis and Identification of Pf14-3-3 Protein as a Histone H3 Phosphorylation Reader in Malaria Parasites

Overview of attention for article published in PLOS ONE, January 2013
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Title
Comprehensive Histone Phosphorylation Analysis and Identification of Pf14-3-3 Protein as a Histone H3 Phosphorylation Reader in Malaria Parasites
Published in
PLOS ONE, January 2013
DOI 10.1371/journal.pone.0053179
Pubmed ID
Authors

Eeshita G. Dastidar, Kristina Dzeyk, Jeroen Krijgsveld, Nicholas A. Malmquist, Christian Doerig, Artur Scherf, Jose-Juan Lopez-Rubio

Abstract

The important role of histone posttranslational modifications, particularly methylation and acetylation, in Plasmodium falciparum gene regulation has been established. However, the role of histone phosphorylation remains understudied. Here, we investigate histone phosphorylation utilizing liquid chromatography and tandem mass spectrometry to analyze histones extracted from asexual blood stages using two improved protocols to enhance preservation of PTMs. Enrichment for phosphopeptides lead to the detection of 14 histone phospho-modifications in P. falciparum. The majority of phosphorylation sites were observed at the N-terminal regions of various histones and were frequently observed adjacent to acetylated lysines. We also report the identification of one novel member of the P. falciparum histone phosphosite binding protein repertoire, Pf14-3-3I. Recombinant Pf14-3-3I protein bound to purified parasite histones. In silico structural analysis of Pf14-3-3 proteins revealed that residues responsible for binding to histone H3 S10ph and/or S28ph are conserved at the primary and the tertiary structure levels. Using a battery of H3 specific phosphopeptides, we demonstrate that Pf14-3-3I preferentially binds to H3S28ph over H3S10ph, independent of modification of neighbouring residues like H3S10phK14ac and H3S28phS32ph. Our data provide key insight into histone phosphorylation sites. The identification of a second member of the histone modification reading machinery suggests a widespread use of histone phosphorylation in the control of various nuclear processes in malaria parasites.

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Geographical breakdown

Country Count As %
United Kingdom 3 4%
France 1 1%
Unknown 69 95%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 19 26%
Researcher 14 19%
Student > Master 7 10%
Student > Postgraduate 4 5%
Student > Doctoral Student 4 5%
Other 13 18%
Unknown 12 16%
Readers by discipline Count As %
Agricultural and Biological Sciences 29 40%
Biochemistry, Genetics and Molecular Biology 18 25%
Chemistry 3 4%
Medicine and Dentistry 2 3%
Computer Science 1 1%
Other 4 5%
Unknown 16 22%