Genetic interactions of yeast eukaryotic translation initiation factor 5a (eIF5A) reveal connections to poly(A)-binding protein and protein kinase C signaling

Detalhes bibliográficos
Autor(a) principal: Valentini, Sandro Roberto [UNESP]
Data de Publicação: 2002
Outros Autores: Casolari, Jason M., Oliveira, Carla C., Silver, Pamela A., McBride, Anne E.
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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spelling 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
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