Abstract

Histone proteins are associated with DNA and form a nucleoprotein structure termed chromatin. Eukaryotic genomes are packed into chromatin for storage and transport of the DNA. To regulate access to DNA for various essential processes such as transcription and translation, histone modifying, DNA modifying and chromatin binding proteins specifically interact with chromatin structures. Here we characterize the specific interaction of the Decondensation factor 31 (Df31) with core histones. Df31 was recently shown to form a complex with snoRNAs and chromatin, to generate accessible higher order structures of chromatin.