Elucidation of nucleosome structural changes based on histone modifications

2015 Fiscal Year Final Research Report

• Project/Area Number: 24370052
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Partial Multi-year Fund
• Section: 一般
• Research Field: Functional biochemistry
• Research Institution: The University of Tokyo
• Principal Investigator: Horikoshi Masami 東京大学, 分子細胞生物学研究所, 准教授 (70242089)
• Project Period (FY): 2012-04-01 – 2016-03-31
• Keywords: ヒストンシャペロン / ヌクレオソーム / 化学修飾 / 構造変換 / ヌクレオソームアセンブリー / ヌクレオソームディスアセンブリー / ヒストン / ヒストンバリアント

Outline of Final Research Achievements

We used a histone-GLibrary that encompasses the nucleosomal DNA entry/exit site to show that six residues form a surface on the structured nucleosome core and regulate H3-K36me3. We also found an interaction between Jhd2 and H2A. Two H2A residues serve as a binding site for Jhd2 and mediate its chromatin association and H3K4 demethylase functions. We described a method to discriminate between the functions of a common subunit in different multisubunit complexes. A common subunit in a multisubunit complex is genetically fused to a subunit that is specific to that complex and point mutated. The resulting phenotype(s) identify the specific function(s) of the subunit in that complex only. We proposed an innovative concept for evolutionary analysis that does not require an outer group. This approach utilizes the similarity in intramolecular direct repeats as an evolutionary measure revealing the degree of similarity between the present offspring genes and their ancestors.

Free Research Field

生化学、分子生物学、遺伝学、構造生物学