DNA interaction Deficiency of RbAp48 protein and memory loss

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the crystal structure of nucleosome core particle h3 , h4 coloured in blue , green respectively.dna coloured gray


in eukaryotic cells, dna wrapped around octamer of histone proteins form nucleosomes, fold higher-order chromatin structures. nucleosome comprises 2 copies of histone h3 , histone h4. these nucleosomes form heterotetramer , bind dna in first step of nucleosome assembly. when dna replicated, nucleosomes need disassembled in front of fork , histones must transferred newly duplicated strands reassembly. studies of in- vivo composition of histone h3 complexes, structural of asf1-h3-h4 complex, have shown histone h3-h4 complexes handled protein dimer.


proteins rbap48 key player in assembly of nucleosomes. rbap48 protein subunit of chromatin-assembly factor-1 (caf-1) complex, assembles histones h3 , h4 onto newly replicated dna initiate nucleosomes assembly. rbap48 protein found in numerous other protein complexes regulation of chromatin structure. studies show rbap48 interacts h3-h4 dimers , imply function of rbap48 involved in numerous process such chromatin assembly, remodeling , modifications; therefore, in many other chromatin-related processes, histones h3-h4 might handled dimer. more generally, seems plausible presence of rbap48 may reflex post-translational modifications of nucleosome. result, can affect activities of neurons , impact memory encoding ability








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