| Literature DB >> 24874291 |
Liesbeth Vossaert1, Paulien Meert1, Ellen Scheerlinck1, Pieter Glibert1, Nadine Van Roy2, Björn Heindryckx3, Petra De Sutter3, Maarten Dhaenens1, Dieter Deforce4.
Abstract
Posttranslational histone modifications are essential features in epigenetic regulatory networks. One of these modifications has remained largely understudied: regulated histone proteolysis. In analogy to the histone H3 clipping during early mouse embryonic stem cell differentiation, we report for the first time that also in human embryonic stem cells this phenomenon takes place in the two different analyzed cell lines. Employing complementary techniques, different cleavage sites could be identified, namely A21, R26 and residue 31. The enzyme responsible for this cleavage is found to be a serine protease. The formation of cleaved H3 follows a considerably variable pattern, depending on the timeframe, culture conditions and culture media applied. Contrary to earlier findings on H3 clipping, our results disconnect the link between declining Oct4 expression and H3 cleavage.Entities:
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Year: 2014 PMID： 24874291 DOI： 10.1016/j.scr.2014.05.002
Source DB: PubMed Journal: Stem Cell Res ISSN： 1873-5061 Impact factor: 2.020