Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification
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Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification. / Tessarz, Peter; Santos-Rosa, Helena; Robson, Sam C; Sylvestersen, Kathrine B; Nelson, Christopher J; Nielsen, Michael L; Kouzarides, Tony.
In: Nature, Vol. 505, 23.01.2014, p. 564-568.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification
AU - Tessarz, Peter
AU - Santos-Rosa, Helena
AU - Robson, Sam C
AU - Sylvestersen, Kathrine B
AU - Nelson, Christopher J
AU - Nielsen, Michael L
AU - Kouzarides, Tony
PY - 2014/1/23
Y1 - 2014/1/23
N2 - Nucleosomes are decorated with numerous post-translational modifications capable of influencing many DNA processes. Here we describe a new class of histone modification, methylation of glutamine, occurring on yeast histone H2A at position 105 (Q105) and human H2A at Q104. We identify Nop1 as the methyltransferase in yeast and demonstrate that fibrillarin is the orthologue enzyme in human cells. Glutamine methylation of H2A is restricted to the nucleolus. Global analysis in yeast, using an H2AQ105me-specific antibody, shows that this modification is exclusively enriched over the 35S ribosomal DNA transcriptional unit. We show that the Q105 residue is part of the binding site for the histone chaperone FACT (facilitator of chromatin transcription) complex. Methylation of Q105 or its substitution to alanine disrupts binding to FACT in vitro. A yeast strain mutated at Q105 shows reduced histone incorporation and increased transcription at the ribosomal DNA locus. These features are phenocopied by mutations in FACT complex components. Together these data identify glutamine methylation of H2A as the first histone epigenetic mark dedicated to a specific RNA polymerase and define its function as a regulator of FACT interaction with nucleosomes.
AB - Nucleosomes are decorated with numerous post-translational modifications capable of influencing many DNA processes. Here we describe a new class of histone modification, methylation of glutamine, occurring on yeast histone H2A at position 105 (Q105) and human H2A at Q104. We identify Nop1 as the methyltransferase in yeast and demonstrate that fibrillarin is the orthologue enzyme in human cells. Glutamine methylation of H2A is restricted to the nucleolus. Global analysis in yeast, using an H2AQ105me-specific antibody, shows that this modification is exclusively enriched over the 35S ribosomal DNA transcriptional unit. We show that the Q105 residue is part of the binding site for the histone chaperone FACT (facilitator of chromatin transcription) complex. Methylation of Q105 or its substitution to alanine disrupts binding to FACT in vitro. A yeast strain mutated at Q105 shows reduced histone incorporation and increased transcription at the ribosomal DNA locus. These features are phenocopied by mutations in FACT complex components. Together these data identify glutamine methylation of H2A as the first histone epigenetic mark dedicated to a specific RNA polymerase and define its function as a regulator of FACT interaction with nucleosomes.
U2 - 10.1038/nature12819
DO - 10.1038/nature12819
M3 - Journal article
C2 - 24352239
VL - 505
SP - 564
EP - 568
JO - Nature
JF - Nature
SN - 0028-0836
ER -
ID: 97269398