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Statements

Subject Item
n2:RIV%2F61388971%3A_____%2F13%3A00422075%21RIV14-MSM-61388971
rdf:type
n3:Vysledek skos:Concept
dcterms:description
As we have shown previously, yeast Mmi1 protein translocates from the cytoplasm to the outer surface of mitochondria when vegetatively growing yeast cells are exposed to oxidative stress. Here we analyzed the effect of heat stress on Mmi1 distribution. We performed domain analyses and found that binding of Mmi1 to mitochondria is mediated by its central alpha-helical domain (V-domain) under all conditions tested. In contrast, the isolated N-terminal flexible loop domain of the protein always displays nuclear localization. Using immunoelectron microscopy we confirmed re-location of Mmi1 to the nucleus and showed association of Mmi1 with intact and heat shock-altered mitochondria. We also show here that mmi1 Delta mutant strains are resistant to robust heat shock with respect to clonogenicity of the cells. To elucidate this phenotype we found that the cytosolic Mmi1 holoprotein re-localized to the nucleus even in cells heat-shocked at 40 degrees C. Upon robust heat shock at 46 degrees C, Mmi1 partly co-localized with the proteasome marker Rpn1 in the nuclear region as well as with the cytoplasmic stress granules defined by Rpg1 (eIF3a). We co-localized Mmi1 also with Bre5, Ubp3 and Cdc48 which are involved in the protein de-ubiquitination machinery, protecting protein substrates from proteasomal degradation. A comparison of proteolytic activities of wild type and mmi1 Delta cells revealed that Mmi1 appears to be an inhibitor of the proteasome. We conclude that one of the physiological functions of the multifunctional protein module, Mmi1, is likely in regulating degradation and/or protection of proteins thereby indirectly regulating the pathways leading to cell death in stressed cells As we have shown previously, yeast Mmi1 protein translocates from the cytoplasm to the outer surface of mitochondria when vegetatively growing yeast cells are exposed to oxidative stress. Here we analyzed the effect of heat stress on Mmi1 distribution. We performed domain analyses and found that binding of Mmi1 to mitochondria is mediated by its central alpha-helical domain (V-domain) under all conditions tested. In contrast, the isolated N-terminal flexible loop domain of the protein always displays nuclear localization. Using immunoelectron microscopy we confirmed re-location of Mmi1 to the nucleus and showed association of Mmi1 with intact and heat shock-altered mitochondria. We also show here that mmi1 Delta mutant strains are resistant to robust heat shock with respect to clonogenicity of the cells. To elucidate this phenotype we found that the cytosolic Mmi1 holoprotein re-localized to the nucleus even in cells heat-shocked at 40 degrees C. Upon robust heat shock at 46 degrees C, Mmi1 partly co-localized with the proteasome marker Rpn1 in the nuclear region as well as with the cytoplasmic stress granules defined by Rpg1 (eIF3a). We co-localized Mmi1 also with Bre5, Ubp3 and Cdc48 which are involved in the protein de-ubiquitination machinery, protecting protein substrates from proteasomal degradation. A comparison of proteolytic activities of wild type and mmi1 Delta cells revealed that Mmi1 appears to be an inhibitor of the proteasome. We conclude that one of the physiological functions of the multifunctional protein module, Mmi1, is likely in regulating degradation and/or protection of proteins thereby indirectly regulating the pathways leading to cell death in stressed cells
dcterms:title
Mmi1, the Yeast Homologue of Mammalian TCTP, Associates with Stress Granules in Heat-Shocked Cells and Modulates Proteasome Activity Mmi1, the Yeast Homologue of Mammalian TCTP, Associates with Stress Granules in Heat-Shocked Cells and Modulates Proteasome Activity
skos:prefLabel
Mmi1, the Yeast Homologue of Mammalian TCTP, Associates with Stress Granules in Heat-Shocked Cells and Modulates Proteasome Activity Mmi1, the Yeast Homologue of Mammalian TCTP, Associates with Stress Granules in Heat-Shocked Cells and Modulates Proteasome Activity
skos:notation
RIV/61388971:_____/13:00422075!RIV14-MSM-61388971
n3:predkladatel
n4:ico%3A61388971
n7:aktivita
n12:I n12:P
n7:aktivity
I, P(7AMB12AT002), P(GAP302/11/0146), P(GAP305/12/0480)
n7:cisloPeriodika
10
n7:dodaniDat
n14:2014
n7:domaciTvurceVysledku
n13:8915466 n13:5768470 n13:4438078
n7:druhVysledku
n15:J
n7:duvernostUdaju
n11:S
n7:entitaPredkladatele
n10:predkladatel
n7:idSjednocenehoVysledku
88631
n7:idVysledku
RIV/61388971:_____/13:00422075
n7:jazykVysledku
n17:eng
n7:klicovaSlova
CONTROLLED TUMOR PROTEIN; SACCHAROMYCES-CEREVISIAE; OXIDATIVE STRESS
n7:klicoveSlovo
n18:CONTROLLED%20TUMOR%20PROTEIN n18:OXIDATIVE%20STRESS n18:SACCHAROMYCES-CEREVISIAE
n7:kodStatuVydavatele
US - Spojené státy americké
n7:kontrolniKodProRIV
[C5A9D4E00CB3]
n7:nazevZdroje
PLoS ONE
n7:obor
n16:EE
n7:pocetDomacichTvurcuVysledku
3
n7:pocetTvurcuVysledku
10
n7:projekt
n9:GAP305%2F12%2F0480 n9:7AMB12AT002 n9:GAP302%2F11%2F0146
n7:rokUplatneniVysledku
n14:2013
n7:svazekPeriodika
8
n7:tvurceVysledku
Malínský, Jan Rinnerthaler, M. Breitenbach, M. Breitenbach-Koller, L. Richter, K. Hašek, Jiří Heeren, G. Lejsková, Renata Groušl, Tomáš Strádalová, Vendula
n7:wos
000326241200040
s:issn
1932-6203
s:numberOfPages
13
n8:doi
10.1371/journal.pone.0077791