BRPF1 mutations reported in the literature include one missense and fourteen frameshifts. Functional studies showed that BRPF1 mutation lead to deletion of structural domains resulting to C-terminal truncations of protein. Indeed, BRPF1 mutations leading to deletion of binding domains resulted in to incapacity to form tetrameric complexes and reduced capacity to stimulate acetyltransferase. In addition, HeLa cells transfected with BRPF1 mutation demonstrated that truncated variants were not able to stimulate K23 acetylation of histone H3. Finally, knockdown of BRPF1 in transgenic mice showed defective H3K23 acetylation in thymus and spleen extracts from theses mouses. The latter suggests ultimately a epigenetic deregulation.
BRPF1