Nucleic Acids Research, 1993, Vol. 21, No. 18 4187-4192
© 1993
MOLECULAR BIOLOGY |
A damage-recognition protein which binds to DNA containing interstrand cross-links is absent or defective in Fanconi anemia, Complementation group A, cells
Department of Laboratory Medicine and Pathology, UMDNJ, New Jersey Medical School and the Graduate School of Biomedical Sciences 185 South Orange Avenue, Newark, NJ 07103 1Fox Chase Cancer Center 7701 burholme Avenue, Philadelphia PA 19111, USA
*To whom correspondence should be addressed
Received June 29, 1993. Revised August 4, 1993. Accepted August 4, 1993.
A DNA binding protein with specificity for DNA containing interstrand cross-links Induced by 4,5‘,8-trlmethylpsoralen (TMP) plus long wavelength ultraviolet (UVA) light has been identified in normal human chromatin. Protein binding to DNA was determined using a gel mobility shift assay and an ollgonucleotide containing a hot spot for formation of psoralen Interstrand cross-links. Specificity of the damage-recognition protein for cross-links was demonstrated both by a positive correlation between level of cross-link formation in DNA and extent of protein binding and by effective competition by treated but not undamaged DNA for the binding protein. Chromatin protein extracts from cells from individuals with the genetic disorder, Fanconi anemia, complementation group A (FA-A), which have decreased ability to repair damage produced by TMP plus UVA light, failed to show any protein binding to TMP plus UVA treated DNA. We have previously shown that these chromatin protein extracts contain a DNA endonuclease complex, pi 4.6, which specifically recognizes and incises DNA containing Interstrand cross-links and which In FA-A cells Is defective In its ability to incise this damaged DNA (Lambert et al. (1992) Mutation Res., 273, 57–71). Together, these findings suggest that the DNA binding protein identified Is involved in recognition and repair of DNA Interstrand cross-links
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