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J Biol Chem, Vol. 274, Issue 31, 21679-21687, July 30, 1999

DNA Ligase III Is Recruited to DNA Strand Breaks by a Zinc Finger Motif Homologous to That of Poly(ADP-ribose) Polymerase
IDENTIFICATION OF TWO FUNCTIONALLY DISTINCT DNA BINDING REGIONS WITHIN DNA LIGASE III

Zachary B. MackeyDagger , Claude Niedergang, Josiane Ménissier-de Murcia, John LeppardDagger , Karin Auparallel , Jingwen Chenparallel , Gilbert de Murcia, and Alan E. TomkinsonDagger

From the Dagger  Department of Molecular Medicine, Institute of Biotechnology, The University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245,  UPR 9003 du Centre National de la Recherche Scientifique, Laboratoire Conventionné avec le Commissariat à l'Energie Atomique, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant, F-67400 Illkirch-Graffenstaden, France, and parallel  Department of Molecular Genetics, Glaxo Wellcome Inc., Research Triangle Park, North Carolina 27709

Mammalian DNA ligases are composed of a conserved catalytic domain flanked by unrelated sequences. At the C-terminal end of the catalytic domain, there is a 16-amino acid sequence, known as the conserved peptide, whose role in the ligation reaction is unknown. Here we show that conserved positively charged residues at the C-terminal end of this motif are required for enzyme-AMP formation. These residues probably interact with the triphosphate tail of ATP, positioning it for nucleophilic attack by the active site lysine. Amino acid residues within the sequence RFPR, which is invariant in the conserved peptide of mammalian DNA ligases, play critical roles in the subsequent nucleotidyl transfer reaction that produces the DNA-adenylate intermediate. DNA binding by the N-terminal zinc finger of DNA ligase III, which is homologous with the two zinc fingers of poly(ADP-ribose) polymerase, is not required for DNA ligase activity in vitro or in vivo. However, this zinc finger enables DNA ligase III to interact with and ligate nicked DNA at physiological salt concentrations. We suggest that in vivo the DNA ligase III zinc finger may displace poly(ADP-ribose) polymerase from DNA strand breaks, allowing repair to occur.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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