Evidence that ubiquitylated H2B corrals hDot1L on the nucleosomal surface to induce H3K79 methylation

Nature Communications

Volumn 7, Issue , 2016, Pages

  Zhou, Linjiao ^a   Holt, Matthew T ^b   Ohashi, Nami ^a   Zhao, Aishan ^a   Müller, Manuel M ^a   Wang, Boyuan ^a,b   Muir, Tom W ^a  

^a PRINCETON UNIVERSITY   (United States)

^b ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H2B; HISTONE H3; LYSINE; DOT1L PROTEIN, HUMAN; HISTONE; METHYLTRANSFERASE; NUCLEOSOME; PROTEIN BINDING; UBIQUITINATED PROTEIN;

AMINO ACID; BIOCHEMISTRY; CYTOGENETICS; DNA; ENZYME; METHYLATION; PROTEIN; PROTEOMICS;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; HISTONE METHYLATION; HISTONE UBIQUITINATION; HUMAN; IN VITRO STUDY; LIQUID CHROMATOGRAPHY; NUCLEOSOME; ONE POT SYNTHESIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN PURIFICATION; SIZE EXCLUSION CHROMATOGRAPHY; TANDEM MASS SPECTROMETRY; UBIQUITINATION; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; METHYLATION; MOLECULAR MODEL; PHYSIOLOGY; PROTEIN CONFORMATION;

GENE EXPRESSION REGULATION, ENZYMOLOGIC; HISTONES; HUMANS; METHYLATION; METHYLTRANSFERASES; MODELS, MOLECULAR; NUCLEOSOMES; PROTEIN BINDING; PROTEIN CONFORMATION; UBIQUITINATED PROTEINS;

EID: 84957547988     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms10589     Document Type: Article

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