Nucleic Acids Research, Vol 26, Issue 2 462-468, Copyright © 1998 by Oxford University Press
GF Moolenaar, RS Uiterkamp, DA Zwijnenburg and N Goosen
The incisions in the DNA at the 3'- and 5'-side of a DNA damage during
nucleotide excision repair in Escherichia coli occur in a complex
consisting of damaged DNA, UvrB and UvrC. The exact requirements for the
two incision events, however, are different. It has previously been shown
that the 3'-incision requires the interaction between the C- terminal
domain of UvrB and a homologous region in UvrC. This interaction, however,
is dispensable for the 5'-incision. Here we show that the C-terminal domain
of the UvrC protein is essential for the 5'- incision, whereas this domain
can be deleted without affecting the 3'- incision. The C-terminal domain of
UvrC is homologous with the C- terminal part of the ERCC1 protein which, in
a complex with XPF, is responsible for the 5'-incision reaction in human
nucleotide excision repair. Both in the UvrC and the ERCC1 domain a
Helix-hairpin-Helix (HhH) motif can be indicated, albeit at different
positions. Such a motif also has been found in a large variety of DNA
binding proteins and it has been suggested to form a structure involved in
non-sequence- specific DNA binding. In contrast to the full length UvrC
protein, a truncated UvrC protein (UvrC554) lacking the entire ERCC1
homology including the HhH motif no longer binds to ssDNA. Analysis of
protein- DNA complexes using bandshift experiments showed that this
putative DNA binding domain of UvrC is required for stabilisation of the
UvrBC-DNA complex after the 3'-incision has taken place. We propose that
after the initial 3'-incision the HhH motif recognises a specific DNA
structure, thereby positioning the catalytic site for the subsequent 5'-
incision reaction.
ARTICLES
The C-terminal region of the Escherichia coli UvrC protein, which is homologous to the C-terminal region of the human ERCC1 protein, is involved in DNA binding and 5'-incision
Laboratory of Molecular Genetics, Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, Einsteinweg 55, PO Box 9502, 2300 RA Leiden, The Netherlands.
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