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The decondensation factor 31 specifically binds to ssRNA but not to ssDNA or dsDNA

Histone proteins are associated with DNA and form a nucleoprotein structure termed chromatin. The chromatin structure allows the eukaryotic genome to be stored and transported but also needs to be accessible to various crucial DNA dependent processes Thus, histone modifying, DNA modifying and chromatin binding proteins specifically interact and regulate chromatin.. Interestingly, many of the chromatin modifying proteins also display RNA binding capacity. Here we characterize the specific interaction of the Decondensation factor 31 (Df31) with nucleic acids. Df31 was recently shown to form be part of a RNA dependent regulating mechanism influencing chromatin structure and function.

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The decondensation factor 31 binds to mono-nucleosomes
The decondensation factor 31 binds to mono-nucleosomes

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The decondensation factor 31 specifically interacts with histones H3 and H4 but not H2A and H2B
The decondensation factor 31 specifically interacts with histones H3 and H4 but not H2A and H2B

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