Int6/eIF3e promotes general translation and Atf1 abundance to modulate Sty1 MAPK-dependent stress response in fission yeast.

2.50
Hdl Handle:
http://hdl.handle.net/10541/56016
Title:
Int6/eIF3e promotes general translation and Atf1 abundance to modulate Sty1 MAPK-dependent stress response in fission yeast.
Authors:
Udagawa, T; Nemoto, N; Wilkinson, Caroline R M; Narashimhan, J; Jiang, L; Watt, S; Zook, A; Jones, Nic; Wek, R; Bähler, J; Asano, K
Abstract:
int-6 is one of the frequent integration sites for mouse mammary tumor viruses. Although its product is the e-subunit of translation initiation factor eIF3, other evidence indicates that it interacts with proteasomes or other proteins to regulate protein stability. Here we report that the fission yeast int6(+) is required for overcoming stress imposed by histidine starvation, using the drug 3-aminotriazole (3AT). Microarray and complementary Northern studies using wild-type, int6Delta or gcn2Delta mutants indicate that 3AT-treated wild-type yeast induces core environmental stress response (CESR) genes in addition to typical general amino acid control (GAAC) genes whose transcription depends on the eIF2 kinase, Gcn2. In agreement with this, Sty1 MAPK and its target transcription factor Atf1, which signal the CESR, are required for overcoming 3AT-induced starvation. We find that Int6 is required for maintaining the basal level of Atf1 and for rapid transcriptional activation of the CESR on 3AT-insult. Pulse labeling experiments indicate that int6Delta significantly slows down de novo protein synthesis. Moreover, Atf1 protein half-life was reduced in int6Delta cells. These effects would account for the compromised Atf1 activity on 3AT-induced stress. Thus, the robust protein synthesis promoted by intact eIF3 appears to be a part of the requisites for sound Sty1 MAPK-dependent signaling governed by the activity of the Atf1 transcription factor.
Affiliation:
Molecular Cellular and Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, Kansas 66506, USA.
Citation:
Int6/eIF3e promotes general translation and Atf1 abundance to modulate Sty1 MAPK-dependent stress response in fission yeast. 2008, 283 (32):22063-75 J. Biol. Chem.
Journal:
The Journal of Biological Chemistry
Issue Date:
8-Aug-2008
URI:
http://hdl.handle.net/10541/56016
DOI:
10.1074/jbc.M710017200
PubMed ID:
18502752
Type:
Article
Language:
en
ISSN:
0021-9258
Appears in Collections:
All Paterson Institute for Cancer Research; Cell Regulation

Full metadata record

DC FieldValue Language
dc.contributor.authorUdagawa, T-
dc.contributor.authorNemoto, N-
dc.contributor.authorWilkinson, Caroline R M-
dc.contributor.authorNarashimhan, J-
dc.contributor.authorJiang, L-
dc.contributor.authorWatt, S-
dc.contributor.authorZook, A-
dc.contributor.authorJones, Nic-
dc.contributor.authorWek, R-
dc.contributor.authorBähler, J-
dc.contributor.authorAsano, K-
dc.date.accessioned2009-03-17T16:58:19Z-
dc.date.available2009-03-17T16:58:19Z-
dc.date.issued2008-08-08-
dc.identifier.citationInt6/eIF3e promotes general translation and Atf1 abundance to modulate Sty1 MAPK-dependent stress response in fission yeast. 2008, 283 (32):22063-75 J. Biol. Chem.en
dc.identifier.issn0021-9258-
dc.identifier.pmid18502752-
dc.identifier.doi10.1074/jbc.M710017200-
dc.identifier.urihttp://hdl.handle.net/10541/56016-
dc.description.abstractint-6 is one of the frequent integration sites for mouse mammary tumor viruses. Although its product is the e-subunit of translation initiation factor eIF3, other evidence indicates that it interacts with proteasomes or other proteins to regulate protein stability. Here we report that the fission yeast int6(+) is required for overcoming stress imposed by histidine starvation, using the drug 3-aminotriazole (3AT). Microarray and complementary Northern studies using wild-type, int6Delta or gcn2Delta mutants indicate that 3AT-treated wild-type yeast induces core environmental stress response (CESR) genes in addition to typical general amino acid control (GAAC) genes whose transcription depends on the eIF2 kinase, Gcn2. In agreement with this, Sty1 MAPK and its target transcription factor Atf1, which signal the CESR, are required for overcoming 3AT-induced starvation. We find that Int6 is required for maintaining the basal level of Atf1 and for rapid transcriptional activation of the CESR on 3AT-insult. Pulse labeling experiments indicate that int6Delta significantly slows down de novo protein synthesis. Moreover, Atf1 protein half-life was reduced in int6Delta cells. These effects would account for the compromised Atf1 activity on 3AT-induced stress. Thus, the robust protein synthesis promoted by intact eIF3 appears to be a part of the requisites for sound Sty1 MAPK-dependent signaling governed by the activity of the Atf1 transcription factor.en
dc.language.isoenen
dc.subject.meshAmino Acids-
dc.subject.meshAmitrole-
dc.subject.meshEukaryotic Initiation Factor-3-
dc.subject.meshGene Expression Profiling-
dc.subject.meshGene Expression Regulation, Fungal-
dc.subject.meshHistidine-
dc.subject.meshMitogen-Activated Protein Kinases-
dc.subject.meshMultigene Family-
dc.subject.meshMutation-
dc.subject.meshProtein Biosynthesis-
dc.subject.meshProteins-
dc.subject.meshSchizosaccharomyces-
dc.subject.meshSchizosaccharomyces Pombe Proteins-
dc.subject.meshSignal Transduction-
dc.titleInt6/eIF3e promotes general translation and Atf1 abundance to modulate Sty1 MAPK-dependent stress response in fission yeast.en
dc.typeArticleen
dc.contributor.departmentMolecular Cellular and Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, Kansas 66506, USA.en
dc.identifier.journalThe Journal of Biological Chemistryen

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