Skip Navigation

Nucleic Acids Research 2004 32(19):5928-5934; doi:10.1093/nar/gkh909
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (304K) Freely available
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 ISI Web of Science
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 (9)
Right arrowRequest Permissions
Citing Articles
Right arrowScopus Links
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Hashimoto, K.
Right arrow Articles by Moriya, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hashimoto, K.
Right arrow Articles by Moriya, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published online 5 November 2004

Nucleic Acids Research, Vol. 32 No. 19 © Oxford University Press 2004; all rights reserved

Futile short-patch DNA base excision repair of adenine:8-oxoguanine mispair

Keiji Hashimoto, Yohei Tominaga1, Yusaku Nakabeppu1 and Masaaki Moriya*

Laboratory of Chemical Biology, Department of Pharmacological Sciences, State University of New York, Stony Brook, NY 11794-8651, USA and 1 Division of Neurofunctional Genomics, Department of Immunobiology and Neuroscience, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan

* To whom correspondence should be addressed. Tel: +1 631 444 3082; Fax: +1 631 444 7641; Email: maki{at}pharm.sunysb.edu

Received September 30, 2004; Accepted October 7, 2004

8-Oxo-7, 8-dihydrodeoxyguanosine (8-oxo-dG), one of the representative oxidative DNA lesions, frequently mispairs with the incoming dAMP during mammalian DNA replication. Mispaired dA is removed by post-replicative base excision repair (BER) initiated by adenine DNA glycosylase, MYH, creating an apurinic (AP) site. The subsequent mechanism ensuring a dC:8-oxo-dG pair, a substrate for 8-oxoguanine DNA glycosylase (OGG1), remains to be elucidated. At the nucleotide insertion step, none of the mammalian DNA polymerases examined exclusively inserted dC opposite 8-oxo-dG that was located in a gap. AP endonuclease 1, which possesses 3'->5' exonuclease activity and potentially serves as a proofreader, did not discriminate dA from dC that was located opposite 8-oxo-dG. However, human DNA ligases I and III joined 3'-dA terminus much more efficiently than 3'-dC terminus when paired to 8-oxo-dG. In reconstituted short-patch BER, repair products contained only dA opposite 8-oxo-dG. These results indicate that human DNA ligases discriminate dC from dA and that MYH-initiated short-patch BER is futile and hence this BER must proceed to long-patch repair, even if it is initiated as short-patch repair, through strand displacement synthesis from the ligation-resistant dC terminus to generate the OGG1 substrate, dC:8-oxo-dG pair.


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
 Proc. Natl. Acad. Sci. USAHome page
B. van Loon and U. Hubscher
An 8-oxo-guanine repair pathway coordinated by MUTYH glycosylase and DNA polymerase {lambda}
PNAS, October 27, 2009; 106(43): 18201 - 18206.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
M. T. Russo, G. De Luca, I. Casorelli, P. Degan, S. Molatore, F. Barone, F. Mazzei, T. Pannellini, P. Musiani, and M. Bignami
Role of MUTYH and MSH2 in the Control of Oxidative DNA Damage, Genetic Instability, and Tumorigenesis
Cancer Res., May 15, 2009; 69(10): 4372 - 4379.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
R. Fazlieva, C. S. Spittle, D. Morrissey, H. Hayashi, H. Yan, and Y. Matsumoto
Proofreading exonuclease activity of human DNA polymerase {delta} and its effects on lesion-bypass DNA synthesis
Nucleic Acids Res., May 1, 2009; 37(9): 2854 - 2866.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
G. Maga, E. Crespan, U. Wimmer, B. van Loon, A. Amoroso, C. Mondello, C. Belgiovine, E. Ferrari, G. Locatelli, G. Villani, et al.
Replication protein A and proliferating cell nuclear antigen coordinate DNA polymerase selection in 8-oxo-guanine repair
PNAS, December 30, 2008; 105(52): 20689 - 20694.
[Abstract] [Full Text] [PDF]

Home page
 Toxicol SciHome page
Y.-S. Pu, K.-Y. Jan, T.-C. Wang, A. S. S. Wang, and J.-R. Gurr
8-Oxoguanine DNA Glycosylase and MutY Homolog Are Involved in the Incision of Arsenite-Induced DNA Adducts
Toxicol. Sci., February 1, 2007; 95(2): 376 - 382.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
A. A. Sartori, G. M. Lingaraju, P. Hunziker, F. K. Winkler, and J. Jiricny
Pa-AGOG, the founding member of a new family of archaeal 8-oxoguanine DNA-glycosylases
Nucleic Acids Res., December 16, 2004; 32(22): 6531 - 6539.
[Abstract] [Full Text] [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.