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Nucleic Acids Res. 1997 Apr 1;25(7):1369-74.

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

Author information

1
Molecular Biology Program, Sloan-Kettering Institute, New York, NY 10021 USA.

Abstract

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.

PMID:
9060431
PMCID:
PMC146593
DOI:
10.1093/nar/25.7.1369
[Indexed for MEDLINE]
Free PMC Article

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