Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling
Autor(a) principal: | |
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Data de Publicação: | 2002 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://www.ncbi.nlm.nih.gov/pubmed/11861547 http://hdl.handle.net/11449/66852 |
Resumo: | The highly conserved eukaryotic translation initiation factor eIF5A has been proposed to have various roles in the cell, from translation to mRNA decay to nuclear protein export. To further our understanding of this essential protein, three temperature-sensitive alleles of the yeast TIF51A gene have been characterized. Two mutant eIF5A proteins contain mutations in a proline residue at the junction between the two eIFSA domains and the third, strongest allele encodes a protein with a single mutation in each domain, both of which are required for the growth defect. The stronger tif51A alleles cause defects in degradation of short-lived mRNAs, supporting a role for this protein in mRNA decay. A multicopy suppressor screen revealed six genes, the overexpression of which allows growth of a tif51A-1 strain at high temperature; these genes include PAB1, PKC1, and PKC1 regulators WSC1, WSC2, and WSC3. Further results suggest that eIFSA may also be involved in ribosomal synthesis and the WSC/PKC1 signaling pathway for cell wall integrity or related processes. |
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Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signalingbinding proteininitiation factor 5Amessenger RNAnuclear proteinproteinprotein kinase Callelecell wallgene interactiongene mutationgene overexpressionhigh temperaturenonhumanpriority journalprotein degradationprotein protein interactionsignal transductionstrain differencetemperature sensitivityyeastAllelesMutation, MissensePeptide Initiation FactorsPoly(A)-Binding ProteinsProtein Kinase CRNA-Binding ProteinsSaccharomyces cerevisiaeSignal TransductionTemperatureEukaryotaFungiMyxogastriaSaccharomycesThe highly conserved eukaryotic translation initiation factor eIF5A has been proposed to have various roles in the cell, from translation to mRNA decay to nuclear protein export. To further our understanding of this essential protein, three temperature-sensitive alleles of the yeast TIF51A gene have been characterized. Two mutant eIF5A proteins contain mutations in a proline residue at the junction between the two eIFSA domains and the third, strongest allele encodes a protein with a single mutation in each domain, both of which are required for the growth defect. The stronger tif51A alleles cause defects in degradation of short-lived mRNAs, supporting a role for this protein in mRNA decay. A multicopy suppressor screen revealed six genes, the overexpression of which allows growth of a tif51A-1 strain at high temperature; these genes include PAB1, PKC1, and PKC1 regulators WSC1, WSC2, and WSC3. Further results suggest that eIFSA may also be involved in ribosomal synthesis and the WSC/PKC1 signaling pathway for cell wall integrity or related processes.Department of Biological Chemistry and Molecular Pharmacology Harvard Medical School, Boston, MA 02115Department of Cancer Biology Dana-Farber Cancer Institute, Boston, MA 02115Department of Biological Sciences School of Pharmacy São Paulo State University, Araraquara, SP, 14801-902Department of Biochemistry Institute of Chemistry University of São Paulo, São Paulo, SP 05508-900Dana-Farber Cancer Institute, 44 Binney St., SM922, Boston, MA 02115Department of Biology Bowdoin College, Brunswick, ME 04011Department of Biological Sciences School of Pharmacy São Paulo State University, Araraquara, SP, 14801-902Harvard Medical SchoolDana-Farber Cancer InstituteUniversidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Bowdoin CollegeValentini, Sandro Roberto [UNESP]Casolari, Jason M.Oliveira, Carla C.Silver, Pamela A.McBride, Anne E.2014-05-27T11:20:26Z2014-05-27T11:20:26Z2002-03-14info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article393-405application/pdfhttp://www.ncbi.nlm.nih.gov/pubmed/11861547Genetics, v. 160, n. 2, p. 393-405, 2002.0016-6731http://hdl.handle.net/11449/66852WOS:0001740976000062-s2.0-00361884482-s2.0-0036188448.pdf5333250355049814Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengGenetics4.0753,484info:eu-repo/semantics/openAccess2024-06-24T13:08:00Zoai:repositorio.unesp.br:11449/66852Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T20:15:23.038989Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling |
title |
Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling |
spellingShingle |
Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling Valentini, Sandro Roberto [UNESP] binding protein initiation factor 5A messenger RNA nuclear protein protein protein kinase C allele cell wall gene interaction gene mutation gene overexpression high temperature nonhuman priority journal protein degradation protein protein interaction signal transduction strain difference temperature sensitivity yeast Alleles Mutation, Missense Peptide Initiation Factors Poly(A)-Binding Proteins Protein Kinase C RNA-Binding Proteins Saccharomyces cerevisiae Signal Transduction Temperature Eukaryota Fungi Myxogastria Saccharomyces |
title_short |
Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling |
title_full |
Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling |
title_fullStr |
Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling |
title_full_unstemmed |
Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling |
title_sort |
Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling |
author |
Valentini, Sandro Roberto [UNESP] |
author_facet |
Valentini, Sandro Roberto [UNESP] Casolari, Jason M. Oliveira, Carla C. Silver, Pamela A. McBride, Anne E. |
author_role |
author |
author2 |
Casolari, Jason M. Oliveira, Carla C. Silver, Pamela A. McBride, Anne E. |
author2_role |
author author author author |
dc.contributor.none.fl_str_mv |
Harvard Medical School Dana-Farber Cancer Institute Universidade Estadual Paulista (Unesp) Universidade de São Paulo (USP) Bowdoin College |
dc.contributor.author.fl_str_mv |
Valentini, Sandro Roberto [UNESP] Casolari, Jason M. Oliveira, Carla C. Silver, Pamela A. McBride, Anne E. |
dc.subject.por.fl_str_mv |
binding protein initiation factor 5A messenger RNA nuclear protein protein protein kinase C allele cell wall gene interaction gene mutation gene overexpression high temperature nonhuman priority journal protein degradation protein protein interaction signal transduction strain difference temperature sensitivity yeast Alleles Mutation, Missense Peptide Initiation Factors Poly(A)-Binding Proteins Protein Kinase C RNA-Binding Proteins Saccharomyces cerevisiae Signal Transduction Temperature Eukaryota Fungi Myxogastria Saccharomyces |
topic |
binding protein initiation factor 5A messenger RNA nuclear protein protein protein kinase C allele cell wall gene interaction gene mutation gene overexpression high temperature nonhuman priority journal protein degradation protein protein interaction signal transduction strain difference temperature sensitivity yeast Alleles Mutation, Missense Peptide Initiation Factors Poly(A)-Binding Proteins Protein Kinase C RNA-Binding Proteins Saccharomyces cerevisiae Signal Transduction Temperature Eukaryota Fungi Myxogastria Saccharomyces |
description |
The highly conserved eukaryotic translation initiation factor eIF5A has been proposed to have various roles in the cell, from translation to mRNA decay to nuclear protein export. To further our understanding of this essential protein, three temperature-sensitive alleles of the yeast TIF51A gene have been characterized. Two mutant eIF5A proteins contain mutations in a proline residue at the junction between the two eIFSA domains and the third, strongest allele encodes a protein with a single mutation in each domain, both of which are required for the growth defect. The stronger tif51A alleles cause defects in degradation of short-lived mRNAs, supporting a role for this protein in mRNA decay. A multicopy suppressor screen revealed six genes, the overexpression of which allows growth of a tif51A-1 strain at high temperature; these genes include PAB1, PKC1, and PKC1 regulators WSC1, WSC2, and WSC3. Further results suggest that eIFSA may also be involved in ribosomal synthesis and the WSC/PKC1 signaling pathway for cell wall integrity or related processes. |
publishDate |
2002 |
dc.date.none.fl_str_mv |
2002-03-14 2014-05-27T11:20:26Z 2014-05-27T11:20:26Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://www.ncbi.nlm.nih.gov/pubmed/11861547 Genetics, v. 160, n. 2, p. 393-405, 2002. 0016-6731 http://hdl.handle.net/11449/66852 WOS:000174097600006 2-s2.0-0036188448 2-s2.0-0036188448.pdf 5333250355049814 |
url |
http://www.ncbi.nlm.nih.gov/pubmed/11861547 http://hdl.handle.net/11449/66852 |
identifier_str_mv |
Genetics, v. 160, n. 2, p. 393-405, 2002. 0016-6731 WOS:000174097600006 2-s2.0-0036188448 2-s2.0-0036188448.pdf 5333250355049814 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Genetics 4.075 3,484 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
393-405 application/pdf |
dc.source.none.fl_str_mv |
Scopus reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1808129180565504000 |