The methylation of the C-terminal region of hnRNPQ (NSAP1) is important for its nuclear localization

dc.creatorPassos, DO
dc.creatorQuaresma, AJC
dc.creatorKobarg, J
dc.date2006
dc.date46935
dc.date2014-11-14T17:07:37Z
dc.date2015-11-26T16:07:41Z
dc.date2014-11-14T17:07:37Z
dc.date2015-11-26T16:07:41Z
dc.date.accessioned2018-03-28T22:56:21Z
dc.date.available2018-03-28T22:56:21Z
dc.identifierBiochemical And Biophysical Research Communications. Academic Press Inc Elsevier Science, v. 346, n. 2, n. 517, n. 525, 2006.
dc.identifier0006-291X
dc.identifierWOS:000238631500018
dc.identifier10.1016/j.bbrc.2006.05.152
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/73635
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/73635
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/73635
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1266194
dc.descriptionProtein arginine methylation is an irreversible post-translational protein modification catalyzed by a family of at least nine different enzymes entitled PRMTs (protein arginine methyl transferases). Although PRMT1 is responsible for 85% of the protein methylation in human cells, its substrate spectrum has not yet been fully characterized nor are the functional consequences of methylation for the protein substrates well understood. Therefore, we set out to employ the yeast two-hybrid system in order to identify new substrate proteins for human PRMT1. We were able to identify nine different PRMT1 interacting proteins involved in different aspects of RNA metabolism, five of which had been previously described either as substrates for PRMT1 or as functionally associated with PRMT1. Among the four new identified possible protein substrates was hnRNPQ3 (NSAP1), a protein whose function has been implicated in diverse steps of mRNA maturation, including splicing, editing, and degradation. By in vitro methylation assays we were able to show that hnRNPQ3 is a substrate for PRMT1 and that its C-terminal RGG box domain is the sole target for methylation. By further studies with the inhibitor of methylation Adox we provide evidence that hnRNPQ1-3 are methylated in vivo. Finally, we demonstrate by immunofluorescence analysis of HeLa cells that the methylation of hnRNPQ is important for its nuclear localization, since Adox treatment causes its re-distribution from the nucleus to the cytoplasm. (c) 2006 Elsevier Inc. All rights reserved.
dc.description346
dc.description2
dc.description517
dc.description525
dc.languageen
dc.publisherAcademic Press Inc Elsevier Science
dc.publisherSan Diego
dc.publisherEUA
dc.relationBiochemical And Biophysical Research Communications
dc.relationBiochem. Biophys. Res. Commun.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectyeast two-hybrid system
dc.subjectprotein arginine methylation
dc.subjectpost-translational modification
dc.subjectprotein-protein interactions
dc.subjectidentification of methylated substrates
dc.subjectsub-cellular localization
dc.subjectRna-binding-protein
dc.subjectArginine N-methyltransferase
dc.subjectSubstrate-specificity
dc.subjectGene-expression
dc.subjectGry-rbp
dc.subjectIn-vivo
dc.subjectInteracts
dc.subjectFamily
dc.subjectIdentification
dc.subjectComplex
dc.titleThe methylation of the C-terminal region of hnRNPQ (NSAP1) is important for its nuclear localization
dc.typeArtículos de revistas


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