Ki-1/57 interacts with PRMT1 and is a substrate for arginine methylation

dc.creatorPassos, DO
dc.creatorBressan, GC
dc.creatorNery, FC
dc.creatorKobarg, J
dc.date2006
dc.dateSEP
dc.date2014-11-16T09:12:58Z
dc.date2015-11-26T16:21:32Z
dc.date2014-11-16T09:12:58Z
dc.date2015-11-26T16:21:32Z
dc.date.accessioned2018-03-28T23:03:31Z
dc.date.available2018-03-28T23:03:31Z
dc.identifierFebs Journal. Blackwell Publishing, v. 273, n. 17, n. 3946, n. 3961, 2006.
dc.identifier1742-464X
dc.identifierWOS:000239858300008
dc.identifier10.1111/j.1742-4658.2006.05399.x
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/60947
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/60947
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/60947
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1267969
dc.descriptionThe human 57 kDa Ki-1 antigen (Ki-1/57) is a cytoplasmic and nuclear protein, associated with Ser/Thr protein kinase activity, and phosphorylated at the serine and threonine residues upon cellular activation. We have shown that Ki-1/57 interacts with chromo-helicase DNA-binding domain protein 3 and with the adaptor/signaling protein receptor of activated kinase 1 in the nucleus. Among the identified proteins that interacted with Ki-1/57 in a yeast two-hybrid system was the protein arginine-methyltransferase-1 (PRMT1). Most interestingly, when PRMT1 was used as bait in a yeast two-hybrid system we were able to identify Ki-1/57 as prey among 14 other interacting proteins, the majority of which are involved in RNA metabolism or in the regulation of transcription. We found that Ki-1/57 and its putative paralog CGI-55 have two conserved Gly/Arg-rich motif clusters (RGG/RXR box, where X is any amino acid) that may be substrates for arginine-methylation by PRMT1. We observed that all Ki-1/57 protein fragments containing RGG/RXR box clusters interact with PRMT1 and are targets for methylation in vitro. Furthermore, we found that Ki-1/57 is a target for methylation in vivo. Using immunofluorescence experiments we observed that treatment of HeLa cells with an inhibitor of methylation, adenosine-2',3'-dialdehyde (Adox), led to a reduction in the cytoplasmic immunostaining of Ki-1/57, whereas its paralog CGI-55 was partially redistributed from the nucleus to the cytoplasm upon Adox treatment. In summary, our data show that the yeast two-hybrid assay is an effective system for identifying novel PRMT arginine-methylation substrates and may be successfully applied to other members of the growing family of PRMTs.
dc.description273
dc.description17
dc.description3946
dc.description3961
dc.languageen
dc.publisherBlackwell Publishing
dc.publisherOxford
dc.publisherInglaterra
dc.relationFebs Journal
dc.relationFEBS J.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectcellular localization
dc.subjectmapping
dc.subjectpost-translational modification
dc.subjectprotein arginine methylation
dc.subjectregulatory protein
dc.subjectRna-binding Protein
dc.subjectMessenger-rna
dc.subjectMethyltransferase
dc.subjectAntigen
dc.subjectSequence
dc.subjectHodgkin
dc.subjectRack1
dc.subjectCells
dc.subjectIdentification
dc.subjectCloning
dc.titleKi-1/57 interacts with PRMT1 and is a substrate for arginine methylation
dc.typeArtículos de revistas


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