Purified Human SUV3p Exhibits Multiple-Substrate Unwinding Activity upon Conformational Change

Biochemistry

Volumn 43, Issue 16, 2004, Pages 4781-4790

  Shu, Zhanyong ^a   Vijayakumar, Sangeetha ^b   Chen, Chi Fen ^b   Chen, Phang Lang ^b   Lee, Wen Hwa ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b Mays Cancer Center at UT Health San Antonio   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDITY; ADENOSINETRIPHOSPHATE; AMINO ACIDS; BIOCATALYSTS; CHROMATOGRAPHIC ANALYSIS; DNA; GLUCOSE; HYDROLYSIS; MUTAGENESIS; ORGANIC COMPOUNDS; PH EFFECTS; PHYSIOLOGICAL MODELS; RNA; SPECTRUM ANALYSIS; YEAST;

NONFERMENTABLE CARBON SOURCE; RNA HELICASE MOTIFS; UNWINDING ACTIVITY;

MOLECULAR BIOLOGY;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALANINE; AMINO ACID; ARGININE; CARBON; DOUBLE STRANDED DNA; DOUBLE STRANDED RNA; GLUCOSE; HELICASE; LYSINE; PROTEIN SUV3; RNA; RNA HELICASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

ACIDITY; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CHROMATOGRAPHY; CIRCULAR DICHROISM; COLONY FORMATION; CONTROLLED STUDY; ENERGY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME PURIFICATION; ENZYME SUBSTRATE; GROWTH; HUMAN; HYDROLYSIS; MUTANT; NONHUMAN; PH; PHENOTYPE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DNA BINDING; PROTEIN EXPRESSION; PROTEIN RNA BINDING; SEQUENCE ANALYSIS; SPECTROSCOPY; STIMULATION; YEAST;

ADENOSINE TRIPHOSPHATASES; AMINO ACID MOTIFS; DEAD-BOX RNA HELICASES; ENZYME ACTIVATION; GENE DELETION; HUMANS; HYDROGEN-ION CONCENTRATION; NUCLEIC ACID HETERODUPLEXES; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; RNA HELICASES; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; STRUCTURAL HOMOLOGY, PROTEIN; SUBSTRATE SPECIFICITY;

SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 1942438570     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0356449     Document Type: Article

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