Glutamine methylation on Histone H2A is an RNA Polymerase I dedicated modification

ABSTRACT: Nucleosomes are decorated with numerous post-translational modifications capable of influencing many DNA processes. Here, we describe a new class of 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 we demonstrate that Fibrillarin is the equivalent enzyme in human cells. Glutamine methylation of H2A is restricted to the nucleolus. Global analysis in yeast, using a H2AQ105me specific antibody, show that this modification is exclusively enriched over the 35S rDNA transcriptional unit. We show that the Q105 residue is part of the binding site for the histone chaperone FACT (Facilitator of Transcription) complex. Methylation of Q105 or its substitution to alanine disrupts binding to FACT in vitro. A yeast strain mutated at Q105 exhibits a defect in histone incorporation and shows increased transcription at rDNA genes. This defect is phenocopied by mutations in FACT that decrease its activity. 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.

ORGANISM(S): Saccharomyces cerevisiae

SUBMITTER: Sam Robson 

PROVIDER: E-MTAB-1447 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress