Post-translational modifications (PTMs) of histones are crucial for transcriptional control, defining positive and negative chromatin territories. A switch of opposing functional significance between acetylation and methylation occurs on many residues. Lysine 120 of H2B is modified by two PTMs: ubiquitination, which is required for further trans-tail H3 methylations and elongation, and acetylation, whose role is less clear. ChIP-Seq with MNase I-treated chromatin indicates that H2BK120ac is present on nucleosomes immediately surrounding the TSS of transcribed or poised units, but not in core promoters. In kinetic ChIP analysis of ER-stress inducible genes, H2BK120ac precedes activation and H2B-ub deposition. Using in vitro acetylation assays, pharmacologic inhibition and RNAi, we established that KAT3 is responsible for H2BK120ac. Interestingly, the global levels of H2B-ub decreased in KAT3-inactivated cells. However, RNF20 recruitment was not impaired by KAT3-inactivation. Our data point at acetylation of Lysine 120 of H2B as an early mark of poised or active state and establish a temporal sequence between acetylation and mono-ubiquitination of this H2B residue.

An acetylation-mono-ubiquitination switch on lysine 120 of H2B / R., Gatta; D., Dolfini; F., Zambelli; Imbriano, Carol; G., Pavesi; R., Mantovani. - In: EPIGENETICS. - ISSN 1559-2308. - ELETTRONICO. - 6:5(2011), pp. 630-637. [10.4161/epi.6.5.15623]

An acetylation-mono-ubiquitination switch on lysine 120 of H2B.

IMBRIANO, Carol;
2011

Abstract

Post-translational modifications (PTMs) of histones are crucial for transcriptional control, defining positive and negative chromatin territories. A switch of opposing functional significance between acetylation and methylation occurs on many residues. Lysine 120 of H2B is modified by two PTMs: ubiquitination, which is required for further trans-tail H3 methylations and elongation, and acetylation, whose role is less clear. ChIP-Seq with MNase I-treated chromatin indicates that H2BK120ac is present on nucleosomes immediately surrounding the TSS of transcribed or poised units, but not in core promoters. In kinetic ChIP analysis of ER-stress inducible genes, H2BK120ac precedes activation and H2B-ub deposition. Using in vitro acetylation assays, pharmacologic inhibition and RNAi, we established that KAT3 is responsible for H2BK120ac. Interestingly, the global levels of H2B-ub decreased in KAT3-inactivated cells. However, RNF20 recruitment was not impaired by KAT3-inactivation. Our data point at acetylation of Lysine 120 of H2B as an early mark of poised or active state and establish a temporal sequence between acetylation and mono-ubiquitination of this H2B residue.
2011
6
5
630
637
An acetylation-mono-ubiquitination switch on lysine 120 of H2B / R., Gatta; D., Dolfini; F., Zambelli; Imbriano, Carol; G., Pavesi; R., Mantovani. - In: EPIGENETICS. - ISSN 1559-2308. - ELETTRONICO. - 6:5(2011), pp. 630-637. [10.4161/epi.6.5.15623]
R., Gatta; D., Dolfini; F., Zambelli; Imbriano, Carol; G., Pavesi; R., Mantovani
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