Elimination of inter-domain interactions increases the cleavage fidelity of the restriction endonuclease DraIII

Protein and Cell

Volumn 5, Issue 5, 2014, Pages 357-368

  Zhuo, Wei ^a   Lai, Xuhui ^b   Zhang, Liqing ^a   Chan, Siu Hong ^c   Li, Fengjuan ^b   Zhu, Zhenyu ^c   Yang, Maojun ^a   Sun, Dapeng ^b  

^a TSINGHUA UNIVERSITY   (China)

^b Shanghai RandD Ctr S   (China)

^c NEW ENGLAND BIOLABS   (United States)

Author keywords

DraIII restriction endonuclease; fidelity; inter domain interaction; site directed mutagenesis; star activity; substrate specificity

Indexed keywords

RESTRICTION ENDONUCLEASE; DNA; ENDODEOXYRIBONUCLEASE DRAIII; RECOMBINANT PROTEIN; TYPE II SITE SPECIFIC DEOXYRIBONUCLEASE;

ARTICLE; CATALYSIS; CRYSTALLIZATION; DIFFERENTIAL SCANNING CALORIMETRY; DNA CLEAVAGE; ENZYME ACTIVITY; GENE MUTATION; HYDROGEN BOND; HYDROLYSIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; THERMODYNAMICS; AMINO ACID SEQUENCE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; SEQUENCE ALIGNMENT; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BASE SEQUENCE; CALORIMETRY, DIFFERENTIAL SCANNING; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DEOXYRIBONUCLEASES, TYPE II SITE-SPECIFIC; DNA; DNA CLEAVAGE; ESCHERICHIA COLI; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY;

EID: 84899456471     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-014-0038-z     Document Type: Article

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