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Sökning: onr:"swepub:oai:gup.ub.gu.se/269207" > The Lsm1-7/Pat1 com...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00003764naa a2200373 4500
001oai:gup.ub.gu.se/269207
003SwePub
008240528s2018 | |||||||||||000 ||eng|
009oai:prod.swepub.kib.ki.se:138896352
024a https://gup.ub.gu.se/publication/2692072 URI
024a https://doi.org/10.1371/journal.pgen.10075632 DOI
024a http://kipublications.ki.se/Default.aspx?queryparsed=id:1388963522 URI
040 a (SwePub)gud (SwePub)ki
041 a eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Garre, Elena,d 1978u Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology4 aut0 (Swepub:gu)xgarre
2451 0a The Lsm1-7/Pat1 complex binds to stress-activated mRNAs and modulates the response to hyperosmotic shock.
264 c 2018-07-30
264 1b Public Library of Science (PLoS),c 2018
520 a RNA-binding proteins (RBPs) establish the cellular fate of a transcript, but an understanding of these processes has been limited by a lack of identified specific interactions between RNA and protein molecules. Using MS2 RNA tagging, we have purified proteins associated with individual mRNA species induced by osmotic stress, STL1 and GPD1. We found members of the Lsm1-7/Pat1 RBP complex to preferentially bind these mRNAs, relative to the non-stress induced mRNAs, HYP2 and ASH1. To assess the functional importance, we mutated components of the Lsm1-7/Pat1 RBP complex and analyzed the impact on expression of osmostress gene products. We observed a defect in global translation inhibition under osmotic stress in pat1 and lsm1 mutants, which correlated with an abnormally high association of both non-stress and stress-induced mRNAs to translationally active polysomes. Additionally, for stress-induced proteins normally triggered only by moderate or high osmostress, in the mutants the protein levels rose high already at weak hyperosmosis. Analysis of ribosome passage on mRNAs through co-translational decay from the 5' end (5P-Seq) showed increased ribosome accumulation in lsm1 and pat1 mutants upstream of the start codon. This effect was particularly strong for mRNAs induced under osmostress. Thus, our results indicate that, in addition to its role in degradation, the Lsm1-7/Pat1 complex acts as a selective translational repressor, having stronger effect over the translation initiation of heavily expressed mRNAs. Binding of the Lsm1-7/Pat1p complex to osmostress-induced mRNAs mitigates their translation, suppressing it in conditions of weak or no stress, and avoiding a hyperresponse when triggered.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
700a Pelechano, Vicentu Karolinska Institutet4 aut
700a Sánchez Del Pino, Manuel4 aut
700a Alepuz, Paula4 aut
700a Sunnerhagen, Per,d 1959u Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology4 aut0 (Swepub:gu)xsuper
710a Göteborgs universitetb Institutionen för kemi och molekylärbiologi4 org
773t PLoS Geneticsd : Public Library of Science (PLoS)g 14:7q 14:7x 1553-7390x 1553-7404
856u https://journals.plos.org/plosgenetics/article/file?id=10.1371/journal.pgen.1007563&type=printable
8564 8u https://gup.ub.gu.se/publication/269207
8564 8u https://doi.org/10.1371/journal.pgen.1007563
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:138896352

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