Phosphoproteomic analysis of mammalian infective Trypanosoma brucei subjected to heat shock suggests atypical mechanisms for thermotolerance

Ooi, Cher P. and Benz, Corinna and Urbaniak, Mick (2020) Phosphoproteomic analysis of mammalian infective Trypanosoma brucei subjected to heat shock suggests atypical mechanisms for thermotolerance. Journal of Proteomics, 219. ISSN 1874-3919

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Abstract

The symptoms of African sleeping sickness, caused by the parasite Trypanosoma brucei, can include periods of fever as high as 41 °C which triggers a heat shock response in the parasite. To capture events involved in sensing and responding to heat shock in the mammalian infective form we have conducted a SILAC-based quantitative proteomic and phosphoproteomic analysis of T. brucei cells treated at 41 °C for 1h. Our analysis identified 193 heat shock responsive phosphorylation sites with an average of 5-fold change in abundance, but only 20 heat shock responsive proteins with average of 1.5-fold change. These data indicate that protein abundance does not rapidly respond (≤1 h) to heat shock, and that the changes observed in phosphorylation site abundance are larger and more widespread. The heat shock responsive phosphorylation sites showed enrichment of RNA binding proteins with putative roles in heat shock response included P-body / stress granules and the eukaryotic translation initiation 4F complex. The ZC3H11-MKT1 complex, which stabilises mRNAs of thermotolerance proteins, appears to represent a key signal integration node in the heat shock response.

Item Type:
Journal Article
Journal or Publication Title:
Journal of Proteomics
Additional Information:
This is the author’s version of a work that was accepted for publication in Journal of Proteomics. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Proteomics, 219, 2020 DOI: 10.1016/j.jprot.2020.103735
Uncontrolled Keywords:
/dk/atira/pure/subjectarea/asjc/1300/1304
Subjects:
ID Code:
142212
Deposited By:
Deposited On:
10 Mar 2020 16:45
Refereed?:
Yes
Published?:
Published
Last Modified:
30 Jul 2020 04:52