{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zarebski M"],"funding":["Ligue Contre le Cancer","Association pour la Recherche sur le Cancer","Research Foundation","Institut National Du Cancer","Tempus Public foundation","Hungarian National Science and Research Foundation","ASCRS Research Foundation","Tempus Közalapítvány","Institut Universitaire de France","Association pour la recherche sur le cancer (ARC)","European Commission","Gustave Roussy","Association pour la recherche sur le cancer","Institut Gustave-Roussy","Institut National du Cancer","European Union","Horizon 2020 Framework Programme","COST EuroCellNet","Association \"Ruban Rose\"; Cancéropôle Ile-de-France","Horizon 2020","Fondation pour la Recherche Médicale","National Science Center","Agence National de la Recherche (ANR)","Ligue contre le Cancer"],"pagination":["1230-1239"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9543561"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["99(12)"],"pubmed_abstract":["It is expected that the subnuclear localization of a protein in a fixed cell, detected by microscopy, reflects its position in the living cell. We demonstrate, however, that some dynamic nuclear proteins can change their localization upon fixation by either crosslinking or non-crosslinking methods. We examined the subnuclear localization of the chromatin architectural protein HMGB1, linker histone H1, and core histone H2B in cells fixed by formaldehyde, glutaraldehyde, glyoxal, ethanol, or zinc salts. We demonstrate that some dynamic, weakly binding nuclear proteins, like HMGB1 and H1, may not only be unexpectedly lost from their original binding sites during the fixation process, but they can also diffuse through the nucleus and eventually bind in nucleoli. Such translocation to nucleoli "],"journal":["Cytometry. Part A : the journal of the International Society for Analytical Cytology"],"pubmed_title":["Translocation of chromatin proteins to nucleoli-The influence of protein dynamics on post-fixation localization."],"pmcid":["PMC9543561"],"funding_grant_id":["2017/27/B/NZ3/01065","CA15214","OTKA K128770","2018/02/X/NZ3/02603"],"pubmed_authors":["Szelest O","Jasinska-Konior K","Bosire R","Wesolowska J","Kepp O","Szabo G","Zarebski M","Dobrucki JW","Kroemer G","Eatmann A"],"additional_accession":[]},"is_claimable":false,"name":"Translocation of chromatin proteins to nucleoli-The influence of protein dynamics on post-fixation localization.","description":"It is expected that the subnuclear localization of a protein in a fixed cell, detected by microscopy, reflects its position in the living cell. We demonstrate, however, that some dynamic nuclear proteins can change their localization upon fixation by either crosslinking or non-crosslinking methods. We examined the subnuclear localization of the chromatin architectural protein HMGB1, linker histone H1, and core histone H2B in cells fixed by formaldehyde, glutaraldehyde, glyoxal, ethanol, or zinc salts. We demonstrate that some dynamic, weakly binding nuclear proteins, like HMGB1 and H1, may not only be unexpectedly lost from their original binding sites during the fixation process, but they can also diffuse through the nucleus and eventually bind in nucleoli. Such translocation to nucleoli ","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Dec","modification":"2025-04-22T12:13:28.366Z","creation":"2025-04-06T00:13:21.869Z"},"accession":"S-EPMC9543561","cross_references":{"pubmed":["34110091"],"doi":["10.1002/cyto.a.24464"]}}