Skip Navigation

This Article
Right arrow Print PDF (1140K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (48)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Treiber, D. K.
Right arrow Articles by Essigmann, J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Treiber, D. K.
Right arrow Articles by Essigmann, J. M.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1992, Vol. 20, No. 21 5805-5810
© 1992


MOLECULAR BIOLOGY

An ultraviolet light-damaged DNA recognition protein absent in xeroderma pigmentosum group E cells binds selectively to pyrimidine (6–4) pyrimidone photoproducts

Daniel K. Treiber, Zhenghuan Chen and John M. Essigmann*

Division of Toxicology and Department of Chemistry, Whitaker College of Health Sciences and Technology, Massachusetts Institute of Technology Cambridge, MA 02139, USA

* To whom correspondence should be addressed

Received June 17, 1992. Revised October 7, 1992. Accepted October 7, 1992.

The binding specificity was defined of a human ultraviolet light-damaged DNA recognition protein (UV-DRP), the activity of which is absent in some xeroderma pigmentosum complementation group E cells. Our results suggest that cyclobutane pyrimidine dimers (CPDs) are not high affinity UV-DRP binding sites—a finding consistent with other reports on this protein (Hirschfeld et al)., (1990) Mol. Cell Biol., 10, 2041 – 2048). A major role for 6–4 photoproducts in UV-DRP binding was suggested in studies showing that irradiated oligonucleotides containing a T4C UV box sequence, which efficiently forms a TC 6–4 photoproduct, was a superior substrate for the UV-DRP when compared to a similar irradiated oligonucleotide having a T5 sequence. The latter sequence forms CPDs at a much higher frequency than 6–4 photoproducts. In a more direct approach, T4C-containing oligonucleotides complexed with the UV-DRP were separated from the unbound oligonucleotide fraction and the frequencies of 6–4 photoproducts in the two DNA populations were compared. The UV-DRP-bound fraction was highly enriched for the 6–4 lesion over the unbound fraction supporting the conclusion that 6–4 photoproducts are the principal binding cues for the UV-DRP.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
Q. Zhao, B. M. Barakat, S. Qin, A. Ray, M. A. El-Mahdy, G. Wani, E.-S. Arafa, S. N. Mir, Q.-E. Wang, and A. A. Wani
The p38 Mitogen-activated Protein Kinase Augments Nucleotide Excision Repair by Mediating DDB2 Degradation and Chromatin Relaxation
J. Biol. Chem., November 21, 2008; 283(47): 32553 - 32561.
[Abstract] [Full Text] [PDF]


Home page
CarcinogenesisHome page
K. Sugasawa
Xeroderma pigmentosum genes: functions inside and outside DNA repair
Carcinogenesis, March 1, 2008; 29(3): 455 - 465.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
M. S. Luijsterburg, J. Goedhart, J. Moser, H. Kool, B. Geverts, A. B. Houtsmuller, L. H. F. Mullenders, W. Vermeulen, and R. van Driel
Dynamic in vivo interaction of DDB2 E3 ubiquitin ligase with UV-damaged DNA is independent of damage-recognition protein XPC
J. Cell Sci., August 1, 2007; 120(15): 2706 - 2716.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. A. El-Mahdy, Q. Zhu, Q.-e. Wang, G. Wani, M. Praetorius-Ibba, and A. A. Wani
Cullin 4A-mediated Proteolysis of DDB2 Protein at DNA Damage Sites Regulates in Vivo Lesion Recognition by XPC
J. Biol. Chem., May 12, 2006; 281(19): 13404 - 13411.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
R. Nishi, Y. Okuda, E. Watanabe, T. Mori, S. Iwai, C. Masutani, K. Sugasawa, and F. Hanaoka
Centrin 2 Stimulates Nucleotide Excision Repair by Interacting with Xeroderma Pigmentosum Group C Protein
Mol. Cell. Biol., July 1, 2005; 25(13): 5664 - 5674.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Y. Fujiwara, C. Masutani, T. Mizukoshi, J. Kondo, F. Hanaoka, and S. Iwai
Characterization of DNA Recognition by the Human UV-damaged DNA-binding Protein
J. Biol. Chem., July 9, 1999; 274(28): 20027 - 20033.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
B. J. Hwang, J. M. Ford, P. C. Hanawalt, and G. Chu
Expression of the p48 xeroderma pigmentosum gene is p53-dependent and is involved in global genomic repair
PNAS, January 19, 1999; 96(2): 424 - 428.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
B. J. Hwang, S. Toering, U. Francke, and G. Chu
p48 Activates a UV-Damaged-DNA Binding Factor and Is Defective in Xeroderma Pigmentosum Group E Cells That Lack Binding Activity
Mol. Cell. Biol., July 1, 1998; 18(7): 4391 - 4399.
[Abstract] [Full Text]


Home page
Mol. Cell. Biol.Home page
V. Otrin, I. Kuraoka, T. Nardo, M. McLenigan, A. P. M. Eker, M. Stefanini, A. S. Levine, and R. D. Wood
Relationship of the Xeroderma Pigmentosum Group E DNA Repair Defect to the Chromatin and DNA Binding Proteins UV-DDB and Replication Protein A
Mol. Cell. Biol., June 1, 1998; 18(6): 3182 - 3190.
[Abstract] [Full Text]


Home page
J. Cell Sci.Home page
V. Otrin, M McLenigan, M Takao, A. Levine, and M Protic
Translocation of a UV-damaged DNA binding protein into a tight association with chromatin after treatment of mammalian cells with UV light
J. Cell Sci., January 5, 1997; 110(10): 1159 - 1168.
[Abstract] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.