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Mediator tail subunits can form amyloid-like aggregates in vivo and affect stress response in yeast

Journal article
Authors Xuefeng Zhu
Lihua Chen
Jonas O P Carlsten
Qian Liu
Junsheng Yang
Beidong Liu
Claes M Gustafsson
Published in Nucleic Acids Research
Volume 43
Issue 15
Pages 7306-7314
ISSN 0305-1048
Publication year 2015
Published at Department of Chemistry and Molecular Biology
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 7306-7314
Language en
Links dx.doi.org/10.1093/nar/gkv629
Keywords environmental-stress, saccharomyces-cerevisiae, genetic-variation, global analysis, budding yeast, prion, protein, transcription, mechanism, complex
Subject categories Cell and Molecular Biology

Abstract

The Med2, Med3 and Med15 proteins form a heterotrimeric subdomain in the budding yeast Mediator complex. This Med15 module is an important target for many gene specific transcription activators. A previous proteome wide screen in yeast identified Med3 as a protein with priogenic potential. In the present work, we have extended this observation and demonstrate that both Med3 and Med15 form amyloid-like protein aggregates under H2O2 stress conditions. Amyloid formation can also be stimulated by overexpression of Med3 or of a glutamine-rich domain present in Med15, which in turn leads to loss of the entire Med15 module from Mediator and a change in stress response. In combination with genome wide transcription analysis, our data demonstrate that amyloid formation can change the subunit composition of Mediator and thereby influence transcriptional output in budding yeast.

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