Characterization of an ATP-dependent DNA ligase encoded by Haemophilus influenzae | Zendy

Chonghui Cheng | Zendy

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Characterization of an ATP-dependent DNA ligase encoded by Haemophilus influenzae

Author(s) -

Chonghui Cheng

Publication year - 1997

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/25.7.1369

Subject(s) - dna ligase , biology , biochemistry , nucleoside triphosphate , ligase chain reaction , dna , transferase , dna ligases , escherichia coli , dna polymerase i , microbiology and biotechnology , rna ligase , enzyme , nucleotide , rna , reverse transcriptase , gene , polymerase chain reaction , multiplex polymerase chain reaction

We report that Haemophilus influenzae encodes a 268 amino acid ATP-dependent DNA ligase. The specificity of Haemophilus DNA ligase was investigated using recombinant protein produced in Escherichia coli. The enzyme catalyzed efficient strand joining on a singly nicked DNA in the presence of magnesium and ATP (Km = 0.2 microM). Other nucleoside triphosphates or deoxynucleoside triphosphates could not substitute for ATP. Haemophilus ligase reacted with ATP in the absence of DNA substrate to form a covalent ligase-adenylate intermediate. This nucleotidyl transferase reaction required a divalent cation and was specific for ATP. The Haemophilus enzyme is the first example of an ATP-dependent DNA ligase encoded by a eubacterial genome. It is also the smallest member of the covalent nucleotidyl transferase superfamily, which includes the bacteriophage and eukaryotic ATP-dependent polynucleotide ligases and the GTP-dependent RNA capping enzymes.

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