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Hsp70-associated chaperones have a critical role in buffering protein production costs.
Farkas, Zoltán; Kalapis, Dorottya; Bódi, Zoltán; Szamecz, Béla; Daraba, Andreea; Almási, Karola; Kovács, Károly; Boross, Gábor; Pál, Ferenc; Horváth, Péter; Balassa, Tamás; Molnár, Csaba; Pettkó-Szandtner, Aladár; Klement, Éva; Rutkai, Edit; Szvetnik, Attila; Papp, Balázs; Pál, Csaba.
Afiliación
  • Farkas Z; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Kalapis D; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Bódi Z; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Szamecz B; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Daraba A; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Almási K; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Kovács K; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Boross G; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Pál F; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Horváth P; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Balassa T; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Molnár C; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Pettkó-Szandtner A; Institute of Plant Biology, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Klement É; Laboratory of Proteomic Research, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Rutkai E; Laboratory of Proteomic Research, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
  • Szvetnik A; Division for Biotechnology, Bay Zoltán Nonprofit Ltd, Budapest, Hungary.
  • Papp B; Division for Biotechnology, Bay Zoltán Nonprofit Ltd, Budapest, Hungary.
  • Pál C; Synthetic and Systems Biology Unit, Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Szeged, Hungary.
Elife ; 72018 01 29.
Article en En | MEDLINE | ID: mdl-29377792
Proteins are necessary for cellular growth. Concurrently, however, protein production has high energetic demands associated with transcription and translation. Here, we propose that activity of molecular chaperones shape protein burden, that is the fitness costs associated with expression of unneeded proteins. To test this hypothesis, we performed a genome-wide genetic interaction screen in baker's yeast. Impairment of transcription, translation, and protein folding rendered cells hypersensitive to protein burden. Specifically, deletion of specific regulators of the Hsp70-associated chaperone network increased protein burden. In agreement with expectation, temperature stress, increased mistranslation and a chemical misfolding agent all substantially enhanced protein burden. Finally, unneeded protein perturbed interactions between key components of the Hsp70-Hsp90 network involved in folding of native proteins. We conclude that specific chaperones contribute to protein burden. Our work indicates that by minimizing the damaging impact of gratuitous protein overproduction, chaperones enable tolerance to massive changes in genomic expression.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Chaperonas Moleculares / Proteínas de Saccharomyces cerevisiae / Metabolismo Energético / Proteínas del Choque Térmico HSP72 Tipo de estudio: Health_economic_evaluation / Risk_factors_studies Idioma: En Revista: Elife Año: 2018 Tipo del documento: Article País de afiliación: Hungria Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / Chaperonas Moleculares / Proteínas de Saccharomyces cerevisiae / Metabolismo Energético / Proteínas del Choque Térmico HSP72 Tipo de estudio: Health_economic_evaluation / Risk_factors_studies Idioma: En Revista: Elife Año: 2018 Tipo del documento: Article País de afiliación: Hungria Pais de publicación: Reino Unido