Highly tolerated amino acid substitutions increase the fidelity of Escherichia coli DNA polymerase I

Journal of Biological Chemistry

Volumn 282, Issue 16, 2007, Pages 12201-12209

  Loh, Ern ^a   Choe, Juno ^a   Loeb, Lawrence A ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; DNA; ENZYME ACTIVITY; ESCHERICHIA COLI; GENES; MUTAGENESIS; SUBSTITUTION REACTIONS;

MUTANT POLYMERASES; POLYMERASE ACTIVITY; PROOFREADING; RANDOM LIBRARY;

AMINO ACIDS;

DNA; DNA DIRECTED DNA POLYMERASE BETA;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; DNA LIBRARY; DNA SYNTHESIS; ESCHERICHIA COLI; MUTATION RATE; NONHUMAN; PHENOTYPE; PLASMID; PLASTICITY; PRIORITY JOURNAL; PROTEIN DOMAIN; AMINO ACID SEQUENCE; BINDING SITE; CATALYSIS; CONFORMATION; DNA REPLICATION; ENZYMOLOGY; METABOLISM; MOLECULAR EVOLUTION; MOLECULAR GENETICS; MUTATION; NUCLEOTIDE SEQUENCE; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY;

ESCHERICHIA COLI;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CATALYSIS; DNA MUTATIONAL ANALYSIS; DNA POLYMERASE I; DNA REPLICATION; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR SEQUENCE DATA; MUTATION; PLASMIDS; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 34249660610     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M611294200     Document Type: Article

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