Histone H4 lysine 16 acetylated isoform synthesis opens new route to biophysical studies
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چکیده
منابع مشابه
ISWI Remodelling of Physiological Chromatin Fibres Acetylated at Lysine 16 of Histone H4
ISWI is the catalytic subunit of several ATP-dependent chromatin remodelling factors that catalyse the sliding of nucleosomes along DNA and thereby endow chromatin with structural flexibility. Full activity of ISWI requires residues of a basic patch of amino acids in the N-terminal 'tail' of histone H4. Previous studies employing oligopeptides and mononucleosomes suggested that acetylation of t...
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Histone post-translational modification heritably regulates gene expression involved in most cellular biological processes. Experimental studies suggest that alteration of histone modifications affects gene expression by changing chromatin structure, causing various cellular responses to environmental influences. Arsenic (As), a naturally occurring element and environmental pollutant, is an est...
متن کاملAcetylated histone H4 is preferentially associated with template-active chromatin.
Chromatin from trout testis at an early stage of development was digested with DNase II (deoxyribonucleate 3'-oligonucleotidohydrolase; EC 3.1.4.6), and the solubilized products were fractionated into Mg2+-soluble and -insoluble components. An examination of the histones from these fractions by one- and two-dimensional polyacrylamide gels showed that the highly acetylated species of histone H4 ...
متن کاملStructure and binding of the H4 histone tail and the effects of lysine 16 acetylationw
The H4 histone tail plays a critical role in chromatin folding and regulation—it mediates strong interactions with the acidic patch of proximal nucleosomes and its acetylation at lysine 16 (K16) leads to partial unfolding of chromatin. The molecular mechanism associated with the H4 tail/acidic patch interactions and its modulation via K16 acetylation remains unknown. Here we employ a combinatio...
متن کاملStructure and binding of the H4 histone tail and the effects of lysine 16 acetylation.
The H4 histone tail plays a critical role in chromatin folding and regulation--it mediates strong interactions with the acidic patch of proximal nucleosomes and its acetylation at lysine 16 (K16) leads to partial unfolding of chromatin. The molecular mechanism associated with the H4 tail/acidic patch interactions and its modulation via K16 acetylation remains unknown. Here we employ a combinati...
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ژورنال
عنوان ژورنال: PROTEOMICS
سال: 2013
ISSN: 1615-9853
DOI: 10.1002/pmic.201300145