2012 Fiscal Year Final Research Report

The role of acetylation of histone variant H2AZ in chromatin dynamics upon DNA damage

Research Project

Project/Area Number	23810015
Research Category	Grant-in-Aid for Research Activity Start-up
Allocation Type	Single-year Grants
Research Field	Risk sciences of radiation/Chemicals
Research Institution	Kyoto University
Principal Investigator	MATSUDA Ryo 京都大学, 放射線生物研究センター, 研究員 (70614155)
Project Period (FY)	2011 – 2012
Keywords	TIP60 複合体 / ヒストン H2AX / ヒストン H2AZ / アセチル化 / DNA 損傷応答
Research Abstract	To understand the role of acetylation in chromatin dynamics upon DNA damage, we purified the DNA helicase TAP54, which is the component of the TIP60 histone acetyltransferase (HAT) complex, from nuclear extract of HeLa cells. We found that TAP54 complex has HAT activity. Mass spetrometry (MS) analysis indicated that histone acetyltranferase, which is different from TIP60, and histone variant H2AZ were identified in the TAP54 complex. Since we have already shown that TIP60 acetylates histone variant H2AX upon DNA damage, these findings suggest that the cross talk between acetylation of H2AX and H2AZ has important roles in DNA damage response.