We show here that histone macroH2A1.2 concentrates at the transcriptionally silent XY body, normally being formed during male meiosis in the mouse. A similar accumulation has earlier been observed on the inactive X chromosomes of somatic adult female mammalian cells by Costanzi and Pehrson (1998). This correspondence in the nature of heterochromatinization of the X chromosomes in males and females adds another property of X chromosome inactivation that is shared by males and females at different phases of their life cycle.
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Histone H2A variants alpha1-extension helix directs RNF168-mediated ubiquitination.
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Department of Radiation Oncology, College of Medicine, University of Arkansas for Medical Sciences, Little Rock, AR, 72205, United States.
Histone ubiquitination plays an important role in the DNA damage response (DDR) pathway. RNF168 catalyzes H2A and H2AX ubiquitination on lysine 13/15 (K13/K15) upon DNA damage and promotes the accrual of downstream repair factors at damaged chromatin. Here, we report that RNF168 ubiquitinates the non-canonical H2A variants H2AZ and macroH2A1/2 at the divergent N-terminal tail lysine residue.
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