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An aggregation-prone mutant of eIF3a forms reversible assemblies escaping spatial control in exponentially growing yeast cells
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SYSNO ASEP 0507898 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title An aggregation-prone mutant of eIF3a forms reversible assemblies escaping spatial control in exponentially growing yeast cells Author(s) Senohrábková, Lenka (MBU-M) RID
Malcová, Ivana (MBU-M) RID, ORCID
Hašek, Jiří (MBU-M) RID, ORCIDSource Title Current Genetics. - : Springer - ISSN 0172-8083
Roč. 65, č. 4 (2019), s. 919-940Number of pages 22 s. Language eng - English Country US - United States Keywords Rpg1 ; eIF3a ; Aggregation Subject RIV EE - Microbiology, Virology OECD category Cell biology R&D Projects GA16-05497S GA ČR - Czech Science Foundation (CSF) Method of publishing Limited access Institutional support MBU-M - RVO:61388971 UT WOS 000475695500016 EID SCOPUS 85061068018 DOI 10.1007/s00294-019-00940-8 Annotation 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. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2020 Electronic address https://link.springer.com/article/10.1007%2Fs00294-019-00940-8
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