Beyond the histone tail

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Beyond the histone tail

Post-translational modifications (PTMs) of histones have been implicated in cellular processes such as transcription, replication and DNA repair. These processes normally involve dynamic changes in chromatin structure and DNA accessibility. Most of the PTMs reported so far map on the histone tails and essentially affect chromatin structure indirectly by recruiting effector proteins. A recent st...

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The tale beyond the tail: histone core domain modifications and the regulation of chromatin structure

Histone post-translational modifications occur, not only in the N-terminal tail domains, but also in the core domains. While modifications in the N-terminal tail function largely through the regulation of the binding of non-histone proteins to chromatin, based on their location in the nucleosome, core domain modifications may also function through distinct mechanisms involving structural altera...

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Histone Proteases: the Tale of Tail Clippers

In the histone code hypothesis histone proteolysis is depicted as a novel kind of irreversible post-translational modifications of histones. Site specific proteolysis of histone is hypothesized as a process for removal of epigenetic signature of histones. However, though there are many reports depicting histone proteolysis, there are very few reports on characterization of a histone protease. I...

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histone acylation beyond acetylation: terra incognita in chromatin biology

histone acetylation, one of the first and best studied histone post-translational modifications (ptms), as well as the factors involved in its deposition (writers), binding (readers) and removal (erasers), have been shown to act at the heart of regulatory circuits controlling essential cellular functions. the identification of a variety of competing histone lysine-modifying acyl groups includin...

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Structural cooperativity in histone H3 tail modifications.

Post-translational modifications of histone H3 tails have crucial roles in regulation of cellular processes. There is cross-regulation between the modifications of K4, K9, and K14 residues. The modifications on these residues drastically promote or inhibit each other. In this work, we studied the structural changes of the histone H3 tail originating from the three most important modifications; ...

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ژورنال

عنوان ژورنال: Nucleus

سال: 2013

ISSN: 1949-1034,1949-1042

DOI: 10.4161/nucl.26051