Nucleic Acids Research, Vol 25, Issue 7 1369-1374, Copyright © 1997 by Oxford University Press
C Cheng and S Shuman
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.
ARTICLES
Characterization of an ATP-dependent DNA ligase encoded by Haemophilus influenzae
Molecular Biology Program, Sloan-Kettering Institute, New York, NY 10021 USA.
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