期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
卷 1833, 期 6, 页码 1329-1337出版社
ELSEVIER
DOI: 10.1016/j.bbamcr.2013.02.022
关键词
Toxoplasma gondii; Small heat shock protein 20; Palmitoylation; Inner membrane complex; Endodyogeny
资金
- ANPCyT [BID 1728 OC-AR PICT 2010-1494]
- PIP grant [2010-0190]
- National Institutes of Health-National Institute of Allergy and Infectious Diseases (NIH-NIAID) [AI083162]
- Fogarty International Center Training Grant [NIH D43TW007888]
- NIH [AI096836]
Toxoplasma gondii is an obligate intracellular parasite and the causative agent of toxoplasmosis. Protein palmitoylation is known to play roles in signal transduction and in enhancing the hydrophobicity of proteins thus contributing to their membrane association. Global inhibition of protein palmitoylation has been shown to affect T. gondii physiology and invasion of the host cell. However, the proteins affected by this modification have been understudied. This paper shows that the small heat shock protein 20 from T. gondii (TgHSP20) is synthesized as a mature protein in the cytosol and is palmitoylated in three cysteine residues. However, its localization at the inner membrane complex (IMC) is dependent only on N-terminal palmitoylation. Absence or incomplete N-terminal palmitoylation causes TgHSP20 to partially accumulate in a membranous structure. Interestingly, TgHSP20 palmitoylation is not responsible for its interaction with the daughter cells IMCs. Together, our data describe the importance of palmitoylation in protein targeting to the IMC in T. gondii. (c) 2013 Elsevier B.V. All rights reserved.
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