eIF3a/Rpg1/Tif32 accumulates in granules in osmotically
stressed cells of Saccharomyces cerevisiae

J 2003

eIF3a/Rpg1/Tif32 accumulates in granules in osmotically stressed cells of Saccharomyces cerevisiae

HAŠEK, Jiří, Ivana JANATOVÁ, Iva SLANINOVÁ a M. ŠPRYNGAR

Základní údaje

Originální název

eIF3a/Rpg1/Tif32 accumulates in granules in osmotically stressed cells of Saccharomyces cerevisiae

Autoři

HAŠEK, Jiří, Ivana JANATOVÁ, Iva SLANINOVÁ a M. ŠPRYNGAR

Vydání

Molecular Biology of the Cell, The American Society for Cell Biology, 2003

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

Genetika a molekulární biologie

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Organizační jednotka

Lékařská fakulta

Klíčová slova anglicky

yeast; osmotic stress; eIF3a/Rpg1/Tif32; Saccharomyces cerevisiae

Štítky

eIF3a/Rpg1/Tif32, osmotic stress, Saccharomyces cerevisiae, Yeast

Změněno: 19. 1. 2004 09:40, prof. MUDr. Iva Slaninová, Ph.D.

Anotace

V originále

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.

Citovat

HAŠEK, Jiří, Ivana JANATOVÁ, Iva SLANINOVÁ a 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, roč. 14/2004, Suppl, s. 450a, 1 s.

@article{492252,
   author = {Hašek, Jiří and Janatová, Ivana and Slaninová, Iva and Špryngar, M.},
   article_number = {Suppl},
   keywords = {yeast; osmotic stress; eIF3a/Rpg1/Tif32; Saccharomyces cerevisiae},
   language = {eng},
   journal = {Molecular Biology of the Cell},
   title = {eIF3a/Rpg1/Tif32 accumulates in granules in osmotically stressed cells of Saccharomyces cerevisiae},
   volume = {14/2004},
   year = {2003}
}

TY  - JOUR
ID  - 492252
AU  - Hašek, Jiří - Janatová, Ivana - Slaninová, Iva - Špryngar, M.
PY  - 2003
TI  - eIF3a/Rpg1/Tif32 accumulates in granules in osmotically stressed cells of Saccharomyces cerevisiae
JF  - Molecular Biology of the Cell
VL  - 14/2004
IS  - Suppl
SP  - 450a
EP  - 450a
PB  - The American Society for Cell Biology
KW  - yeast
KW  - osmotic stress
KW  - eIF3a/Rpg1/Tif32
KW  - Saccharomyces cerevisiae
N2  - 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.
ER  -

HAŠEK, Jiří, Ivana JANATOVÁ, Iva SLANINOVÁ a M. ŠPRYNGAR. eIF3a/Rpg1/Tif32 accumulates in granules in osmotically stressed cells of Saccharomyces cerevisiae. \textit{Molecular Biology of the Cell}. The American Society for Cell Biology, 2003, roč.~14/2004, Suppl, s.~450a, 1 s.

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