000056249 001__ 56249
000056249 005__ 20210121114539.0
000056249 0247_ $$2doi$$a10.1073/pnas.1508040112
000056249 0248_ $$2sideral$$a91487
000056249 037__ $$aART-2015-91487
000056249 041__ $$aeng
000056249 100__ $$aGonzález-Arzola, K.
000056249 245__ $$aStructural basis for inhibition of the histone chaperone activity of SET/TAF-Iß by cytochrome c
000056249 260__ $$c2015
000056249 5060_ $$aAccess copy available to the general public$$fUnrestricted
000056249 5203_ $$aChromatin is pivotal for regulation of the DNA damage process insofar as it influences access to DNA and serves as a DNA repair docking site. Recent works identify histone chaperones as key re- gulators of damaged chromatin’s transcriptional activity. However, understanding how chaperones are modulated during DNA damage response is still challenging. This study reveals that the histone chap- erone SET/TAF-Iß interacts with cytochrome c following DNA damage. Specifically, cytochrome c is shown to be translocated into cell nuclei upon induction of DNA damage, but not upon stimulation of the death receptor or stress-induced pathways. Cytochrome c was found to competitively hinder binding of SET/TAF-Iß to core histones, thereby locking its histone-binding domains and inhibiting its nucle- osome assembly activity. In addition, we have used NMR spectros- copy, calorimetry, mutagenesis, and molecular docking to provide an insight into the structural features of the formation of the complex between cytochrome c and SET/TAF-Iß. Overall, these findings estab- lish a framework for understanding the molecular basis of cyto- chrome c-mediated blocking of SET/TAF-Iß, which subsequently may facilitate the development of new drugs to silence the oncogenic effect of SET/TAF-Iß’s histone chaperone activity.
000056249 536__ $$9info:eu-repo/grantAgreement/ES/MINECO/BFU2012-31670$$9info:eu-repo/grantAgreement/ES/MINECO/BFU2013-47064-P$$9info:eu-repo/grantAgreement/ES/MINECO/SAF2012-32824
000056249 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc$$uhttp://creativecommons.org/licenses/by-nc/3.0/es/
000056249 590__ $$a9.423$$b2015
000056249 591__ $$aMULTIDISCIPLINARY SCIENCES$$b4 / 62 = 0.065$$c2015$$dQ1$$eT1
000056249 592__ $$a6.814$$b2015
000056249 593__ $$aMultidisciplinary$$c2015$$dQ1
000056249 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000056249 700__ $$aDíaz-Moreno, I.
000056249 700__ $$aCano-González, A.
000056249 700__ $$aDíaz-Quintana, A.
000056249 700__ $$0(orcid)0000-0001-5702-4538$$aVelázquez-Campoy, A.$$uUniversidad de Zaragoza
000056249 700__ $$aMoreno-Beltrán, B.
000056249 700__ $$aLópez-Rivas, A.
000056249 700__ $$aDe la Rosa, Miguel A.
000056249 700__ $$aFersht, A.R.
000056249 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000056249 773__ $$g112, 32 (2015), 9908-9913$$pProc. Natl. Acad. Sci.$$tProceedings of the National Academy of Sciences$$x0027-8424
000056249 8564_ $$s1383592$$uhttps://zaguan.unizar.es/record/56249/files/texto_completo.pdf$$yVersión publicada
000056249 8564_ $$s146060$$uhttps://zaguan.unizar.es/record/56249/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000056249 909CO $$ooai:zaguan.unizar.es:56249$$particulos$$pdriver
000056249 951__ $$a2021-01-21-11:15:19
000056249 980__ $$aARTICLE