Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36

Journal of Biological Chemistry

Volumn 282, Issue 4, 2007, Pages 2450-2455

  Shi, Xiaobing ^a   Kachirskaia, Ioulia ^a   Walter, Kay L ^a   Kuo, Jen Hao A ^a   Lake, Aimee ^b   Davrazou, Foteini ^c   Chan, Steve M ^d   Martin, David G E ^e   Fingerman, Ian M ^f   Briggs, Scott D ^f   Howe, LeAnn ^e   Utz, Paul J ^d   Kutateladze, Tatiana G ^c   Lugovskoy, Alexey A ^g,h   Bedford, Mark T ^b   Gozani, Or ^a  

^a STANFORD UNIVERSITY   (United States)

^b UNIVERSITY OF TEXAS   (United States)

^c UNIVERSITY OF COLORADO   (United States)

^d STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^e UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^f PURDUE UNIVERSITY   (United States)

^g HARVARD MEDICAL SCHOOL   (United States)

^h BIOGEN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING MODULES; CHROMATIN; HISTONE; STRUCTURAL MODELING;

AMINO ACIDS; BIOCHEMISTRY; GENES; LIGANDS; YEAST;

PROTEINS;

HISTONE H3; LYSINE; PHD FINGER PROTEIN; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; HISTONE; HOMEODOMAIN PROTEIN; PROTEOME; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; BINDING AFFINITY; GENOME; GENOMICS; METHYLATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN MOTIF; PROTEIN PROCESSING; PROTEIN STRUCTURE; PROTEOMICS; SACCHAROMYCES CEREVISIAE; AMINO ACID SEQUENCE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; PROTEIN TERTIARY STRUCTURE;

EUKARYOTA; SACCHAROMYCES CEREVISIAE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; DNA-BINDING PROTEINS; HISTONES; HOMEODOMAIN PROTEINS; LYSINE; METHYLATION; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEOME; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 34047248383     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C600286200     Document Type: Article

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