000056825 001__ 56825
000056825 005__ 20200221144255.0
000056825 0247_ $$2doi$$a10.1038/srep32114
000056825 0248_ $$2sideral$$a96287
000056825 037__ $$aART-2016-96287
000056825 041__ $$aeng
000056825 100__ $$aFernández-Rivero, N.
000056825 245__ $$aA Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility
000056825 260__ $$c2016
000056825 5060_ $$aAccess copy available to the general public$$fUnrestricted
000056825 5203_ $$aNucleoplasmin (NP) is an abundant histone chaperone in vertebrate oocytes and embryos involved in storing and releasing maternal histones to establish and maintain the zygotic epigenome. NP has been considered a H2A-H2B histone chaperone, and recently it has been shown that it can also interact with H3-H4. However, its interaction with different types of histones has not been quantitatively studied so far. We show here that NP binds H2A-H2B, H3-H4 and linker histones with K d values in the subnanomolar range, forming different complexes. Post-translational modifications of NP regulate exposure of the polyGlu tract at the disordered distal face of the protein and induce an increase in chaperone affinity for all histones. The relative affinity of NP for H2A-H2B and linker histones and the fact that they interact with the distal face of the chaperone could explain their competition for chaperone binding, a relevant process in NP-mediated sperm chromatin remodelling during fertilization. Our data show that NP binds H3-H4 tetramers in a nucleosomal conformation and dimers, transferring them to DNA to form disomes and tetrasomes. This finding might be relevant to elucidate the role of NP in chromatin disassembly and assembly during replication and transcription.
000056825 536__ $$9info:eu-repo/grantAgreement/ES/MINECO/BFU2013-47064-P
000056825 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000056825 590__ $$a4.259$$b2016
000056825 591__ $$aMULTIDISCIPLINARY SCIENCES$$b10 / 63 = 0.159$$c2016$$dQ1$$eT1
000056825 592__ $$a1.691$$b2016
000056825 593__ $$aMultidisciplinary$$c2016$$dQ1
000056825 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000056825 700__ $$aFranco, A.
000056825 700__ $$0(orcid)0000-0001-5702-4538$$aVelázquez-Campoy, A.$$uUniversidad de Zaragoza
000056825 700__ $$aAlonso, E.
000056825 700__ $$aMuga, A.
000056825 700__ $$aPrado, A.
000056825 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000056825 773__ $$g6 (2016), 32114 [14 pp.]$$pSci. rep.$$tSCIENTIFIC REPORTS$$x2045-2322
000056825 8564_ $$s1684626$$uhttps://zaguan.unizar.es/record/56825/files/texto_completo.pdf$$yVersión publicada
000056825 8564_ $$s116506$$uhttps://zaguan.unizar.es/record/56825/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000056825 909CO $$ooai:zaguan.unizar.es:56825$$particulos$$pdriver
000056825 951__ $$a2020-02-21-13:30:04
000056825 980__ $$aARTICLE