The JmjN domain of Jhd2 is important for its protein stability, and the plant homeodomain (PHD) finger mediates its chromatin association independent of H3K4 methylation

Journal of Biological Chemistry

Volumn 285, Issue 32, 2010, Pages 24548-24561

  Huang, Fu ^a   Chandrasekharan, Mahesh B ^a   Chen, Yi Chun ^a   Bhaskara, Srividya ^a   Hiebert, Scott W ^a   Sun, Zu Wen ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLATION; AMINO ACIDS; CHROMOSOMES; GENE EXPRESSION; GENE EXPRESSION REGULATION; METHYLATION; YEAST;

CATALYTIC DOMAINS; CHROMATIN STRUCTURE; DEMETHYLASE; DOMAIN-CONTAINING PROTEINS; DYNAMIC PROCESS; E3 LIGASE; HISTONE LYSINE METHYLATION; HOMEODOMAIN; IN-VIVO; INTER-DOMAIN; INTRINSIC ACTIVITIES; MENTAL RETARDATION; N-TERMINALS; NUCLEOSOMES; PROTEIN LEVEL; PROTEIN STABILITY;

PROTEINS;

HISTONE 3 LYSINE 4; HOMEODOMAIN PROTEIN; PLANT HOMEODOMAIN FINGER PROTEIN; PROTEIN JHD2; PROTEIN JMJN; PROTEIN NOT4; PROTEIN SMCX; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; UNCLASSIFIED ENZYME; CHROMATIN; HISTONE; HISTONE DEMETHYLASE; JHD2 PROTEIN, S CEREVISIAE; NUCLEOSOME; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CELL FRACTIONATION; CHROMATIN; CONTROLLED STUDY; FUNGAL STRAIN; GENE MUTATION; HUMAN; IN VIVO STUDY; MENTAL DEFICIENCY; NONHUMAN; NUCLEOSOME; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INDUCTION; PROTEIN INTERACTION; PROTEIN METHYLATION; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; WESTERN BLOTTING; CHEMISTRY; ENZYME ACTIVE SITE; HELA CELL LINE; METABOLISM; METHYLATION; MUTATION; SACCHAROMYCES CEREVISIAE;

CATALYTIC DOMAIN; CHROMATIN; HELA CELLS; HISTONES; HUMANS; JUMONJI DOMAIN-CONTAINING HISTONE DEMETHYLASES; METHYLATION; MUTATION; NUCLEOSOMES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SUBCELLULAR FRACTIONS;

EID: 77955291830     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.117333     Document Type: Article

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