Charge-based interaction conserved within histone H3 lysine 4 (H3K4) methyltransferase complexes is needed for protein stability, histone methylation, and gene expression

Journal of Biological Chemistry

Volumn 287, Issue 4, 2012, Pages 2652-2665

  Mersman, Douglas P ^a   Du, Hai Ning ^a   Fingerman, Ian M ^a   South, Paul F ^a   Briggs, Scott D ^a  

^a Purdue University   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DOMAIN-CONTAINING PROTEINS; HISTONE H3; HISTONE METHYLATION; METHYLTRANSFERASES; MULTISUBUNIT COMPLEXES; PROTEIN INTERACTION; PROTEIN LEVEL; PROTEIN STABILITY; TELOMERES;

ALKYLATION; AMINO ACIDS; CELL GROWTH; COMPLEXATION; GENE EXPRESSION; GROWTH KINETICS; METHYLATION; YEAST;

PROTEINS;

BINDING PROTEIN; HISTONE H3; HISTONE H3 LYSINE 4 METHYLTRANSFERASE; METHYLTRANSFERASE; PROTEIN SET1; PROTEIN SWD1; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL GROWTH; CONTROLLED STUDY; GENE EXPRESSION; HISTONE METHYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; TELOMERE; YEAST;

GENE EXPRESSION REGULATION; HISTONE-LYSINE N-METHYLTRANSFERASE; HISTONES; HUMANS; METHYLATION; MULTIENZYME COMPLEXES; NUCLEAR PROTEINS; PROTEIN STABILITY; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

MAMMALIA;

EID: 84856068282     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.280867     Document Type: Article

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