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J Biol Chem, Vol. 274, Issue 42, 30094-30100, October 15, 1999
From the Department of Biology and Rosenstiel Basic Medical
Sciences Research Center, Brandeis University,
Waltham, Massachusetts 02254-9110
DNA exonucleases are critical for DNA
replication, repair, and recombination. In the bacterium
Escherichia coli there are 14 DNA exonucleases including
exonucleases I-IX (including the two DNA polymerase I exonucleases),
RecJ exonuclease, SbcCD exonuclease, RNase T, and the exonuclease
domains of DNA polymerase II and III. Here we report the discovery and
characterization of a new E. coli exonuclease, exonuclease
X. Exonuclease X is a member of a superfamily of proteins that have
homology to the 3'-5' exonuclease proofreading subunit (DnaQ) of
E. coli DNA polymerase III. We have engineered and purified
a (His)6-exonuclease X fusion protein and characterized its
activity. Exonuclease X is a potent distributive exonuclease, capable
of degrading both single-stranded and duplex DNA with 3'-5' polarity.
Its high affinity for single-strand DNA and its rapid catalytic rate
are similar to the processive exonucleases RecJ and exonuclease I. Deletion of the exoX gene exacerbated the UV sensitivity of
a strain lacking RecJ, exonuclease I, and exonuclease VII. When
overexpressed, exonuclease X is capable of substituting for exonuclease
I in UV repair. As we have proposed for the other single-strand DNA
exonucleases, exonuclease X may facilitate recombinational repair by
pre-synaptic and/or post-synaptic DNA degradation.
Exonuclease X of Escherichia coli
A NOVEL 3'-5' DNase AND DnaQ SUPERFAMILY MEMBER INVOLVED
IN DNA REPAIR
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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