Open AccessIdentification of Plasmodium falciparum nuclear proteins by mass spectrometry and proposed protein annotation
Author(s) -
Sylvie Briquet,
Asma Ourimi,
Cédric Pionneau,
Juliana Silva Bernardes,
Alessandra Carbone,
Solenne Chardonnet,
Catherine Vaquero
Publication year - 2018
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0205596
Subject(s) - biology , ribosomal protein , proteome , plasmodium falciparum , nuclear protein , proteomics , ribosome biogenesis , computational biology , cell nucleus , ribosome , protein targeting , microbiology and biotechnology , genetics , cytoplasm , gene , membrane protein , transcription factor , rna , membrane , malaria , immunology
The nuclear proteome of Plasmodium falciparum results from the continual shuttle of proteins between the cell cytoplasm—nucleus and vice versa . Using shotgun proteomics tools, we explored the nuclear proteins of mixed populations of Plasmodium falciparum extracted from infected erythrocytes. We combined GeLC-MS/MS and 2D-LC-MS/MS with a peptide ion exclusion procedure in order to increase the detection of low abundant proteins such as those involved in gene expression. We have identified 446 nuclear proteins covering all expected nuclear protein families involved in gene regulation. All structural ribosomal (40S and 60S) proteins were identified which is consistent with the nuclear localization of ribosomal biogenesis. Proteins involved in the translation machinery were also found suggesting that translational events might occur in the nucleus in P . falciparum as previously hypothesized in eukaryotes. These data were compared to the protein list established by PlasmoDB and submitted to Plasmobase a recently reported Plasmodium annotation website to propose new functional putative annotation of several unknown proteins found in the nuclear extracts.