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Review

Histone H3 Lysine 56 Acetylation: A New Twist in the Chromosome Cycle

Anil Ozdemir, Hiroshi Masumoto, Paul Fitzhjohn, Alain Verreault and Colin Logie

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Several recent reports have identified lysine 56 (K56) as a novel site of acetylation in yeast histone H3. K56 acetylation is predicted to disrupt some of the histone-DNA interactions at the entry and exit points of the nucleosome core particle. This modification occurs in virtually all the newly synthesised histones that are deposited into chromatin during S-phase. Cells with mutations that block K56 acetylation show increased genome instability and hypersensitivity to genotoxic agents that interfere with replication. Removal of K56 acetylation takes place in the G2/M phase of the cell cycle and is dependent upon Hst3 and Hst4, two proteins that are related to the NAD+-dependent histone deacetylase Sir2. In response to DNA damage checkpoint activation during S-phase, expression of Hst3/Hst4 is delayed to extend the window of opportunity in which K56 acetylation can act in the DNA damage response. The high abundance of histone H3 K56 acetylation, its regulation and strategic location in the nucleosome core particle raise a number of fascinating issues that we discuss here.

Authors

Anil Ozdemir

Radboud University; Nijmegen, The Netherlands

Hiroshi Masumoto

Osaka University;Osaka, Japan

Paul Fitzhjohn

Cancer Research UK; London UK

Alain Verreault

Université de Montréal; Montréal, Québec, Canada

Colin Logie

Radboud University; Nijmegen, The Netherlands

This is an open-access article

 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.