Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification

Nature

Volumn 505, Issue 7484, 2014, Pages 564-568

  Tessarz, Peter ^a,b   Santos Rosa, Helena ^a,b   Robson, Sam C ^a,b   Sylvestersen, Kathrine B ^c   Nelson, Christopher J ^a,b,d   Nielsen, Michael L ^c   Kouzarides, Tony ^a,b  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^c University of Copenhagen   (Denmark)

^d UNIVERSITY OF VICTORIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

35S RIBOSOMAL DNA; ALANINE; CHAPERONE; DACTINOMYCIN; DNA DIRECTED RNA POLYMERASE; FACILITATOR OF CHROMATIN TRANSCRIPTION; FIBRILLARIN; FUNGAL PROTEIN; GLUTAMINE; HISTONE H2A; HISTONE H2AQ104; HISTONE H2AQ105; METHYLTRANSFERASE; NOP1 PROTEIN; RIBOSOME DNA; SMALL INTERFERING RNA; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

AMINO ACID; ANTIBODY; BIOCHEMISTRY; CHROMOSOME; DNA; ENZYME ACTIVITY; FUNCTIONAL ROLE; GENOMICS; HOMINID; METHYLATION; MUTATION; PROTEIN; YEAST;

ANIMAL CELL; ARTICLE; BINDING SITE; BIOGENESIS; CHROMATIN IMMUNOPRECIPITATION; DNA SEQUENCE; ENZYME ACTIVITY; GENE LOCUS; GENOTYPE; HISTONE METHYLATION; HISTONE MODIFICATION; HUMAN; HUMAN CELL; IN VITRO STUDY; LIQUID SCINTILLATION COUNTING; NONHUMAN; NUCLEOLUS; NUCLEOSOME; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN PURIFICATION; RIBOSOME; TANDEM MASS SPECTROMETRY; TEMPERATURE SENSITIVE MUTANT; WESTERN BLOTTING; YEAST;

ALANINE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; CELL NUCLEOLUS; CHROMATIN; CHROMOSOMAL PROTEINS, NON-HISTONE; DNA, RIBOSOMAL; EPISTASIS, GENETIC; GLUTAMINE; HISTONES; HUMANS; METHYLATION; METHYLTRANSFERASES; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; MULTIPROTEIN COMPLEXES; NUCLEAR PROTEINS; NUCLEOSOMES; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; RIBONUCLEOPROTEINS, SMALL NUCLEOLAR; RNA; RNA POLYMERASE I; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUBSTRATE SPECIFICITY; TRANSCRIPTION, GENETIC;

EID: 84892785163     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12819     Document Type: Article

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