Replacement of all arginine residues with canavanine in MazF-bs mRNA interferase changes its specificity

Journal of Biological Chemistry

Volumn 288, Issue 11, 2013, Pages 7564-7571

  Ishida, Yojiro ^a   Park, Jung Ho ^a,b   Mao, Lili ^a   Yamaguchi, Yoshihiro ^a   Inouye, Masayori ^a  

^a RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

^b RUTGERS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; ARGININE RESIDUE; BACILLUS SUBTILIS; FUNCTIONAL PROTEINS; MASS SPECTROMETRY ANALYSIS; PRODUCTION SYSTEM; RECOGNITION SEQUENCE; RNA CLEAVAGE;

ARGININE; ESCHERICHIA COLI; MASS SPECTROMETRY; RNA;

PROTEINS;

ADENINE; ARGININE; BACTERIAL PROTEIN; CANAVANINE; CYTOSINE; MAZF PROTEIN; MESSENGER RNA; UNCLASSIFIED DRUG; URACIL;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS SUBTILIS; BACTERIAL GENE; CODON; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; GENE SEQUENCE; MASS SPECTROMETRY; MAZF GENE; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RNA CLEAVAGE; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ARGININE; BACILLUS SUBTILIS; BASE SEQUENCE; BINDING, COMPETITIVE; CANAVANINE; CIRCULAR DICHROISM; DNA PRIMERS; DNA-BINDING PROTEINS; ENDORIBONUCLEASES; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; MASS SPECTROMETRY; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLASMIDS; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; RNA INTERFERENCE; RNA, MESSENGER; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 84875129963     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.434969     Document Type: Article

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