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J Biol Chem, Vol. 273, Issue 28, 17517-17524, July 10, 1998
From the Department of Biochemistry and Biophysics, P.O. Box
644660, Washington State University, Pullman,
Washington 99164-4660
The fate of nucleosomes during nucleotide
excision repair is unclear. We have used organomercurial chromatography
to capture accessible thiol groups of proteins at (or near) nascent
repair sites in normal and xeroderma pigmentosum (group C) human cells. The reactive groups include cysteine 110 of histone H3, which is
exposed in unfolded nucleosomes. Immediately after UV irradiation and a
short pulse labeling of repair patches, intact nuclei were digested
with restriction enzymes to release ~18% of the chromatin into
soluble fragments, which are enriched (~4-fold) in a constitutively transcribed gene. Upon organomercurial affinity fractionation, ~1.8%
of the soluble chromatin remains bound in high salt (0.5 M NaCl) and is released with dithiothreitol. In
normal cell chromatin, this fraction is enriched in nascent repair
patches (1.5-1.8-fold) over the unbound fraction. This enrichment
decreases following short chase periods with a time course similar to
the loss of enhanced nuclease sensitivity of these regions
(t 1/2
Nucleosome Unfolding during DNA Repair in Normal and Xeroderma
Pigmentosum (Group C) Human Cells
30 min). Much less
enrichment of nascent repair patches is observed in the thiol-reactive
fraction from XPC cells, which repair primarily the transcribed strand
of active genes. These results suggest that transient nucleosome
unfolding occurs during nucleotide excision repair in normal human
cells, and this unfolding may require the XPC protein.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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