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J. Virol., 03 1997, 1931-1937, Vol 71, No. 3
Copyright © 1997, American Society for Microbiology

Characterization of an ATP-dependent DNA ligase encoded by Chlorella virus PBCV-1

CK Ho, JL Van Etten and S Shuman
Molecular Biology Program, Sloan-Kettering Institute, New York, New York 10021, USA.

We report that Chlorella virus PBCV-1 encodes a 298-amino-acid ATP- dependent DNA ligase. The PBCV-1 enzyme is the smallest member of the covalent nucleotidyl transferase superfamily, which includes the ATP- dependent polynucleotide ligases and the GTP-dependent RNA capping enzymes. The specificity of PBCV-1 DNA ligase was investigated by using purified recombinant protein. The enzyme catalyzed efficient strand joining on a singly nicked DNA in the presence of magnesium and ATP (Km, 75 microM). Other nucleoside triphosphates or deoxynucleoside triphosphates could not substitute for ATP. PBCV-1 ligase was unable to ligate across a 2-nucleotide gap and ligated poorly across a 1- nucleotide gap. A native gel mobility shift assay showed that PBCV-1 DNA ligase discriminated between nicked and gapped DNAs at the substrate-binding step. These findings underscore the importance of a properly positioned 3' OH acceptor terminus in substrate recognition and reaction chemistry.


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