An aggregation-prone mutant of eIF3a forms reversible assemblies escaping spatial control in exponentially growing yeast cells
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články
Grantová podpora
16-05497S
Grantov? Agentura ?esk? Republiky
GACU1180213
Grantov? Agentura, Univerzita Karlova
PubMed
30715564
DOI
10.1007/s00294-019-00940-8
PII: 10.1007/s00294-019-00940-8
Knihovny.cz E-zdroje
- Klíčová slova
- Actin, Aggregation, Asymmetric segregation, Hsp40, Hsp70, Myo2, Rpg1/eIF3a, Yeast,
- MeSH
- eukaryotický iniciační faktor 3 genetika MeSH
- lidé MeSH
- mikrofilamenta genetika MeSH
- mitochondrie MeSH
- mutace MeSH
- myosin typu V genetika MeSH
- proteinové agregáty genetika MeSH
- proteiny tepelného šoku HSP40 genetika MeSH
- proteiny tepelného šoku HSP70 genetika MeSH
- Saccharomyces cerevisiae - proteiny genetika MeSH
- Saccharomyces cerevisiae genetika růst a vývoj MeSH
- těžké řetězce myosinu genetika MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- eukaryotický iniciační faktor 3 MeSH
- MYO2 protein, S cerevisiae MeSH Prohlížeč
- myosin typu V MeSH
- proteinové agregáty MeSH
- proteiny tepelného šoku HSP40 MeSH
- proteiny tepelného šoku HSP70 MeSH
- RPG1 protein, S cerevisiae MeSH Prohlížeč
- Saccharomyces cerevisiae - proteiny MeSH
- těžké řetězce myosinu MeSH
Cells have elaborated a complex strategy to maintain protein homeostasis under physiological as well as stress conditions with the aim to ensure the smooth functioning of vital processes and producing healthy offspring. Impairment of one of the most important processes in living cells, translation, might have serious consequences including various brain disorders in humans. Here, we describe a variant of the translation initiation factor eIF3a, Rpg1-3, mutated in its PCI domain that displays an attenuated translation efficiency and formation of reversible assemblies at physiological growth conditions. Rpg1-3-GFP assemblies are not sequestered within mother cells only as usual for misfolded-protein aggregates and are freely transmitted from the mother cell into the bud although they are of non-amyloid nature. Their bud-directed transmission and the active movement within the cell area depend on the intact actin cytoskeleton and the related molecular motor Myo2. Mutations in the Rpg1-3 protein render not only eIF3a but, more importantly, also the eIF3 core complex prone to aggregation that is potentiated by the limited availability of Hsp70 and Hsp40 chaperones. Our results open the way to understand mechanisms yeast cells employ to cope with malfunction and aggregation of essential proteins and their complexes.
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