Identification of a functional hotspot on ubiquitin required for stimulation of methyltransferase activity on chromatin

Proceedings of the National Academy of Sciences of the United States of America

Volumn 112, Issue 33, 2015, Pages 10365-10370

  Holt, Matthew T ^a   David, Yael ^b   Pollock, Sam ^b,d   Tang, Zhanyun ^a   Jeon, Jongcheol ^c   Kim, Jaehoon ^c   Roeder, Robert G ^a   Muir, Tom W ^b  

^a ROCKEFELLER UNIVERSITY   (United States)

^b PRINCETON UNIVERSITY   (United States)

^c Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

^d UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Chromatin; Dot1L; Epigenetics; Protein chemistry; Ubiquitin

Indexed keywords

ARGININE; DISULFIDE; DOT1 PROTEIN; EPITOPE; HISTONE H2B; HISTONE H3; METHYLTRANSFERASE; UBIQUITIN; UNCLASSIFIED DRUG; CHROMATIN; DOT1L PROTEIN, HUMAN; HISTONE; LYSINE; NUCLEOSOME; PROTEIN BINDING;

ARTICLE; BACULOVIRIDAE; CHROMATIN; CIRCULAR DICHROISM; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; FLUORESCENCE RESONANCE ENERGY TRANSFER; HETERONUCLEAR SINGLE QUANTUM COHERENCE; HISTONE METHYLATION; HISTONE UBIQUITINATION; HUMAN; HUMAN CELL; MAMMAL CELL; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTON NUCLEAR MAGNETIC RESONANCE; SACCHAROMYCES CEREVISIAE; SF9 CELL LINE; SURFACE PROPERTY; WILD TYPE; AMINO ACID SEQUENCE; CHEMISTRY; GENETIC EPIGENESIS; METHYLATION; MUTATION; PROCEDURES; PROTEIN ENGINEERING; PROTEIN PROCESSING; SEQUENCE HOMOLOGY; SOFTWARE; STRUCTURE ACTIVITY RELATION; UBIQUITINATION;

AMINO ACID SEQUENCE; CHROMATIN; EPIGENESIS, GENETIC; HISTONES; HUMANS; LYSINE; METHYLATION; METHYLTRANSFERASES; MUTATION; NUCLEOSOMES; PROTEIN BINDING; PROTEIN ENGINEERING; PROTEIN PROCESSING, POST-TRANSLATIONAL; SEQUENCE HOMOLOGY, AMINO ACID; SOFTWARE; STRUCTURE-ACTIVITY RELATIONSHIP; SURFACE PROPERTIES; UBIQUITIN; UBIQUITINATION;

EID: 84940181324     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1504483112     Document Type: Article

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