【摘 要】
：
HBO1,a member of the MYST family histone acetyltransferases(HATs),is required for global acetylation of H3K14 and embryonic development.It functions in multisubunit complexes comprising of HBO1,a BRPF
【机 构】
：
National Center for Protein Science Shanghai,State Key Laboratory of Molecular Biology,Institute of
【出 处】
：
中国生物化学与分子生物学会2016年全国学术会议
论文部分内容阅读
HBO1,a member of the MYST family histone acetyltransferases(HATs),is required for global acetylation of H3K14 and embryonic development.It functions in multisubunit complexes comprising of HBO1,a BRPF1/2/3 or JADE1/2/3 scaffold protein,and two accessory proteins.BRPF2 has been suggested to be important for the HAT activity of HBO1 towards H3K14.Here we demonstrated that BRPF2 can directly regulate the HAT activity of HBO1 towards free H3 and H4 and nucleosomal H3.Particularly,a short N-terminal region of BRPF2 is sufficient for binding to HBO1 and stimulating its HAT activity towards H3K14.The crystal structure of the MYST domain of HBO1 in complex with this segment of BRPF2 together with the biochemical and cell biological data revealed the key residues responsible for the HBO1-BRPF2 interaction.In addition,we found that two negatively charged patches of BRPF2 play important roles in histone binding and stimulation of the HAT activity of HBO1.Our data together indicate that the stimulatory effect of BRPF2 is attributed to its cooperative binding with both HBO1 and histone H3.These findings provide new insight into the molecular mechanism underlying the regulation of the HAT activity of HBO1 by BRPF2 and possibly other scaffold proteins.
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