HAŠEK, Jiří, Ivana JANATOVÁ, Iva SLANINOVÁ and M. ŠPRYNGAR. eIF3a/Rpg1/Tif32 accumulates in granules in osmotically stressed cells of Saccharomyces cerevisiae. Molecular Biology of the Cell. The American Society for Cell Biology, 2003, 14/2004, Suppl, p. 450a, 1 pp.
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Basic information
Original name eIF3a/Rpg1/Tif32 accumulates in granules in osmotically stressed cells of Saccharomyces cerevisiae
Authors HAŠEK, Jiří, Ivana JANATOVÁ, Iva SLANINOVÁ and M. ŠPRYNGAR.
Edition Molecular Biology of the Cell, The American Society for Cell Biology, 2003.
Other information
Original language English
Type of outcome Article in a journal
Field of Study Genetics and molecular biology
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
Organization unit Faculty of Medicine
Keywords in English yeast; osmotic stress; eIF3a/Rpg1/Tif32; Saccharomyces cerevisiae
Tags eIF3a/Rpg1/Tif32, osmotic stress, Saccharomyces cerevisiae, Yeast
Changed by Changed by: prof. MUDr. Iva Slaninová, Ph.D., učo 2105. Changed: 19/1/2004 09:40.
Abstract
EIF3a/Rpg1/Tif32p is the essential subunit of the translation initiation factor eIF3 core complex of Saccharomyces cerevisiae. Besides interactions within the eIF3 complex, Rpg1p physically interacts with the actin-associated protein Sla2/End4/Mop2 and partially co-localizes with microtubules in cells fixed for immunofluorescence. Roles for these cytoskeletal interactions are still unknown. To monitor distribution of Rpg1p in living cells we prepared a C-terminal Rpg1-EGFP fusion. We found that Rpg1-EGFP was uniformly distributed in the cytoplasm of exponentially growing cells. Nevertheless, in osmotically stressed cells, Rpg1-EGFP re-localized to fluorescent granules dominantly associated with the bud tip and the neck between the mother and daughter cells. Disruption of microtubules and actin microfilaments, or the absence of Sla2p did not significantly affect formation, number or distribution of Rpg1-EGFP stress granules. In immunofluorescence, the cells treated with 1M NaCl for 60 minutes displayed Rpg1p granules and depolymerized microtubules. Distribution of the protein Elo3, a marker for endoplasmic reticulum, was not changed. The accumulation of Rpg1p in granules of stressed cells was confirmed by electron microscopy using immunogold labeling. We suggest that Rpg1/Tif32p mediates formation of stress granules. This work was financed by grant GACR 204/02/1424 to JH and Institutional Research Concept No. AV0Z5020903.
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