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Biochim Biophys Acta. 2016 Apr;1864(4):400-8. doi: 10.1016/j.bbapap.2016.01.010. Epub 2016 Jan 26.

Identification of new palmitoylated proteins in Toxoplasma gondii.

Author information

1
Laboratorio de Parasitología Molecular, Instituto de Investigaciones Biotecnológicas-Instituto Tecnológico de Chascomús (IIB-INTECH), Universidad Nacional de San Martín (UNSAM) - Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Intendente Marino Km 8.2, B7130 Chascomús, Provincia de Buenos Aires, Argentina.
2
Department of Biology and Vermont Genetics Network Proteomics Facility, University of Vermont, 120A Marsh Life Science Building, Burlington, VT 05405-0086, USA.
3
Laboratório de Ultraestrutura Celular Hertha Meyer, Instituto de Biofísica, Carlos Chagas Filho and Instituto Nacional de Ciência e Tecnologia em Biologia Estrutural e Bioimagens, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
4
Laboratorio de Parasitología Molecular, Instituto de Investigaciones Biotecnológicas-Instituto Tecnológico de Chascomús (IIB-INTECH), Universidad Nacional de San Martín (UNSAM) - Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Intendente Marino Km 8.2, B7130 Chascomús, Provincia de Buenos Aires, Argentina. Electronic address: mcorvi@intech.gov.ar.

Abstract

Protein palmitoylation has been shown to be an important post-translational modification in eukaryotic cells. This modification alters the localization and/or the function of the targeted protein. In recent years, protein palmitoylation has risen in importance in apicomplexan parasites as well. In Toxoplasma gondii, some proteins have been reported to be modified by palmitate. With the development of new techniques that allow the isolation of palmitoylated proteins, this significant post-translational modification has begun to be studied in more detail in T. gondii. Here we describe the palmitoylome of the tachyzoite stage of T. gondii using a combination of the acyl-biotin exchange chemistry method and mass spectrometry analysis. We identified 401 proteins found in multiple cellular compartments, with a wide range of functions that vary from metabolic processes, gliding and host-cell invasion to even regulation of transcription and translation. Besides, we found that more rhoptry proteins than the ones already described for Toxoplasma are palmitoylated, suggesting an important role for this modification in the invasion mechanism of the host-cell. This study documents that protein palmitoylation is a common modification in T. gondii that could have an impact on different cellular processes.

KEYWORDS:

Acyl-biotin exchange; Host-cell invasion; Palmitoylome; Protein identification; Rhoptry; Toxoplasma gondii

PMID:
26825284
PMCID:
PMC4857766
DOI:
10.1016/j.bbapap.2016.01.010
[Indexed for MEDLINE]
Free PMC Article

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