Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro

Biochemical Journal

Volumn 467, Issue 3, 2015, Pages 507-515

  Li, Hong Tao ^a   Gong, Ting ^a   Zhou, Zhen ^a   Liu, Yu Ting ^a   Cao, Xiongwen ^a   He, Yongning ^a   Chen, Charlie Degui ^a   Zhou, Jin Qiu ^a,b  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

^b SHANGHAITECH UNIVERSITY   (China)

Author keywords

Arginine methyltransferase; Dimer; Histone H3R2; Hmt1; Yeast

Indexed keywords

ARGININE; GENOMIC DNA; HISTONE H3; HYBRID PROTEIN; MONOCLONAL ANTIBODY; POLYCLONAL ANTIBODY; HISTONE; HMT1 PROTEIN, S CEREVISIAE; PROTEIN ARGININE METHYLTRANSFERASE; RECOMBINANT PROTEIN; REPRESSOR PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; ASYMMETRIC CATALYSIS; CARBOXY TERMINAL SEQUENCE; DIMERIZATION; DNA TEMPLATE; ENZYME ACTIVITY; FUSION GENE; GEL FILTRATION CHROMATOGRAPHY; GENE; GENE AMPLIFICATION; GENE SILENCING; HETEROCHROMATIN; HISTONE METHYLATION; IN VITRO STUDY; IN VIVO STUDY; MYELOMA CELL; NONHUMAN; OLIGOMERIZATION; OPEN READING FRAME; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS; SOUTHERN BLOTTING; TELOMERE; URA3 GENE; WESTERN BLOTTING; WILD TYPE; YEAST; YEAST HMT1; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; FUNGAL GENE; GENE DELETION; GENETICS; METABOLISM; METHYLATION; MOLECULAR GENETICS; PROTEIN DOMAIN; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ARGININE; CATALYTIC DOMAIN; GENE DELETION; GENES, FUNGAL; HISTONES; METHYLATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN-ARGININE N-METHYLTRANSFERASES; RECOMBINANT PROTEINS; REPRESSOR PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

EID: 84932127297     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20141437     Document Type: Article

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