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dc.contributor.authorMUNARI, F. M.pt_BR
dc.contributor.authorREVERS, L. F.pt_BR
dc.contributor.authorCARDONE, J. M.pt_BR
dc.contributor.authorIMMICH, B. F.pt_BR
dc.contributor.authorMOURA, D. J.pt_BR
dc.contributor.authorGUECHEVA, T. N.pt_BR
dc.contributor.authorBONATTO, D.pt_BR
dc.contributor.authorLAURINO, J. P.pt_BR
dc.contributor.authorSAFFI, J.pt_BR
dc.contributor.authorBRENDEL, M.pt_BR
dc.contributor.authorHENRIQUES, J. A. P.pt_BR
dc.date.accessioned2016-02-22T12:38:32Z-
dc.date.available2016-02-22T12:38:32Z-
dc.date.created2014-08-28pt_BR
dc.date.issued2014pt_BR
dc.identifier.citationJournal of Photochemistry and Photobiology B: Biology, v. 130, p. 241-253, 2014.pt_BR
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/993657pt_BR
dc.descriptionBy isolating putative binding partners through the two-hybrid system (THS) we further extended the characterization of the specific interstrand cross-link (ICL) repair gene PSO2 of Saccharomyces cerevisiae. Nine fusion protein products were isolated for Pso2p using THS, among them the Sak1 kinase, which interacted with the C-terminal b-CASP domain of Pso2p. Comparison of mutagen-sensitivity phenotypes of pso2D, sak1D and pso2Dsak1D disruptants revealed that SAK1 is necessary for complete WT-like repair. The epistatic interaction of both mutant alleles suggests that Sak1p and Pso2p act in the same pathway of controlling sensitivity to DNA-damaging agents. We also observed that Pso2p is phosphorylated by Sak1 kinase in vitro and co-immunoprecipitates with Sak1p after 8-MOP+UVA treatment. Survival data after treatment of pso2D, yku70D and yku70Dpso2D with nitrogen mustard, PSO2 and SAK1 with YKU70 or DNL4 single-, double- and triple mutants with 8-MOP+UVA indicated that ICL repair is independent of YKu70p and DNL4p in S. cerevisiae. Furthermore, a non-epistatic interaction was observed between MRE11, PSO2 and SAK1 genes after ICL induction, indicating that their encoded proteins act on the same substrate, but in distinct repair pathways. In contrast, an epistatic interaction was observed for PSO2 and RAD52, PSO2 and RAD50, PSO2 and XRS2 genes in 8-MOP+UVA treated exponentially growing cells.pt_BR
dc.language.isoporpt_BR
dc.rightsopenAccesspt_BR
dc.subjectLigações cruzadas interfilamentarespt_BR
dc.subjectPso2pt_BR
dc.subjectSak1pt_BR
dc.subjectInterstrand crosslinkpt_BR
dc.titleSak1 kinase interacts with Pso2 nuclease in response to DNA damage induced by interstrand crosslink-inducing agents in Saccharomyces cerevisiae.pt_BR
dc.typeArtigo de periódicopt_BR
dc.date.updated2019-04-02T11:11:11Zpt_BR
dc.subject.thesagroSaccharomyces cerevisiaept_BR
dc.subject.thesagroDNApt_BR
dc.subject.nalthesaurusCrosslinkingpt_BR
dc.description.notesDOI 10.1016/j.jphotobiol.2013.11.024pt_BR
riaa.ainfo.id993657pt_BR
riaa.ainfo.lastupdate2019-04-02 -03:00:00pt_BR
dc.contributor.institutionFernanda M. Munari; LUIS FERNANDO REVERS, CNPUV; Jacqueline M. Cardone; Bruna F. Immich; Dinara J. Moura; Temenouga N. Guecheva; Diego Bonatto; Jomar P. Laurino; Jenifer Saffi; Martin Brendel; João A.P. Henriques.pt_BR
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