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Evidence for a dynamic role of the linker histone variant H1x during retinoic acid‐induced differentiation of NT2 cells
Author(s) -
Shahhoseini Maryam,
Favaedi Raha,
Baharvand Hossein,
Sharma Vikram,
Stunnenberg Hendrik G
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.10.041
Subject(s) - histone h1 , histone h2a , histone , chromatin immunoprecipitation , retinoic acid , histone methyltransferase , chromatin , histone code , histone methylation , cellular differentiation , microbiology and biotechnology , biology , chromatin remodeling , chemistry , gene expression , genetics , nucleosome , gene , dna methylation , promoter
The dynamics of chromatin structure are tightly regulated by multiple epigenetic mechanisms such as histone modifications and incorporation of histone variants. In the current work, differentiation of an embryonal carcinoma cell line, NT2, was induced by retinoic acid, and total histone proteins were compared throughout this process. The results showed a significant change in expression level of a variant of H1 histone named H1x. Chromatin immunoprecipitation coupled with real‐time PCR analysis demonstrated a preferential incorporation of this protein in the regulatory region of Nanog , a marker gene of stemness that is significantly suppressed in differentiated cells. This finding reveals a dynamic role of H1x in differentiation, and implies a repressive role for this histone variant.