Chaperone requirements for biosynthesis of the trypanosome variant surface glycoprotein.

ABSTRACT:

Background

Trypanosoma brucei does not respond transcriptionally to several endoplasmic reticulum (ER) stress conditions, including tunicamycin or dithiothreitol, indicating the absence of a conventional unfolded protein response. This suggests divergent mechanisms for quality control (QC) of ER protein folding and export may be present in trypanosomes. As the variant surface glycoprotein (VSG) represents approximately 90% of trypanosome plasma membrane protein, it is possible that VSG has evolved to fold efficiently to minimize ER folding burden.

Methodology/principal findings

We demonstrate the presence of a QC system by pharmacological inhibition of the trypanosome 26S proteasome. This indicates active proteasome-mediated VSG turnover as approximately 2.5 fold more VSG is

SUBMITTER: Field MC 

PROVIDER: S-EPMC2797082 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature