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(Received for publication, June 24, 1996)
From the Imperial Cancer Research Fund, Clare Hall Laboratories,
South Mimms, Hertfordshire EN6 3LD, United Kingdom
A human cDNA encoding a previously
unrecognized DNA ligase IV has been identified (Wei, Y.-F.,
Robins, P., Carter, K., Caldecott, K., Pappin, D. J. C., Yu, G.-L.,
Wang, R.-P., Shell, B. K., Nash, R. A., Schär, P., Barnes,
D. E., Haseltine, W. A., and Lindahl, T. (1995) Mol. Cell.
Biol. 15, 3206-3216). Antibodies have been raised against
predicted peptide sequences of DNA ligase IV and used to identify the
enzyme during purification from HeLa cell nuclei. The 96-kDa DNA ligase
IV and the 103-kDa DNA ligase III co-migrate during SDS-polyacrylamide
gel electrophoresis and have similar column fractionation properties,
which complicates the distinction between the two enzymes, but they
have been separated by Mono S liquid chromatography. During initial
size fractionation by gel chromatography in 1 M NaCl, DNA
ligase IV elutes in the same position as the DNA ligase III-XRCC1
protein complex, indicating that DNA ligase IV is also bound to another
protein or occurs as a dimer. DNA ligase IV has been purified free from
other DNA ligases, and its enzymatic properties have been
examined. The purified protein effectively joins single-strand breaks
in a double-stranded polydeoxynucleotide in an ATP-dependent
reaction. The substrate specificity of DNA ligase IV differs from those
of the other two cloned human DNA ligases, I and III, with regard to
their ability to join the hybrid substrates oligo(dT)·poly(rA) and
oligo(rA)·poly(dT). DNA ligase IV occurs in part as an
enzyme-adenylate complex in HeLa cell nuclear extracts.
Volume 271, Number 39,
Issue of September 27, 1996
pp. 24257-24261
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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