Source:http://linkedlifedata.com/resource/pubmed/id/21542867
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
2011-6-27
|
pubmed:abstractText |
Saccharomyces cerevisiae can import iron through a high-affinity system consisting of the Ftr1/Fet3-mediated reductive pathway and the siderophore-mediated non-reductive one. Expression of components of the high-affinity system is controlled by the Aft1 transcriptional factor. In this study we show that, upon oxidative stress, Aft1 is transitorily internalized into the nucleus, followed by transcription activation of components of its regulon. In these conditions, the mRNA levels of the genes of the non-reductive pathway become increased, while those of FTR1 and FET3 remain low because of destabilization of the mRNAs. Consequently, the respective protein levels also remain low. Such mRNA destabilization is mediated by the general 5'-3' mRNA decay pathway and is independent of the RNA binding protein Cth2. Yeast cells are hypersensitive to peroxides in growth conditions where only the high-affinity reductive pathway is functional for iron assimilation. On the contrary, peroxide does not affect growth when iron uptake occurs exclusively through the non-reductive pathway. This reinforces the idea that upon oxidative stress S. cerevisiae cells redirect iron assimilation through the non-reductive pathway to minimize oxidative damage by the ferrous ions, which are formed during iron import through the Ftr1/Fet3 complexes.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ceruloplasmin,
http://linkedlifedata.com/resource/pubmed/chemical/FET3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/FTR1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidants,
http://linkedlifedata.com/resource/pubmed/chemical/RCS1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
1365-2958
|
pubmed:author | |
pubmed:copyrightInfo |
© 2011 Blackwell Publishing Ltd.
|
pubmed:issnType |
Electronic
|
pubmed:volume |
81
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
232-48
|
pubmed:meshHeading |
pubmed-meshheading:21542867-Ceruloplasmin,
pubmed-meshheading:21542867-Gene Expression Regulation, Fungal,
pubmed-meshheading:21542867-Hydrogen Peroxide,
pubmed-meshheading:21542867-Iron,
pubmed-meshheading:21542867-Membrane Transport Proteins,
pubmed-meshheading:21542867-Oxidants,
pubmed-meshheading:21542867-Oxidative Stress,
pubmed-meshheading:21542867-RNA Stability,
pubmed-meshheading:21542867-Regulon,
pubmed-meshheading:21542867-Saccharomyces cerevisiae,
pubmed-meshheading:21542867-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:21542867-Transcription Factors
|
pubmed:year |
2011
|
pubmed:articleTitle |
The oxidative stress response in yeast cells involves changes in the stability of Aft1 regulon mRNAs.
|
pubmed:affiliation |
Departament de Ciències Mèdiques Bàsiques, IRBLleida, Universitat de Lleida, Montserrat Roig 2, 25008 Lleida, Spain.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|