Skip Navigation


Nucleic Acids Research Advance Access originally published online on March 29, 2007
Nucleic Acids Research 2007 35(8):2463-2472; doi:10.1093/nar/gkm075
This Article
Right arrow Full Text Freely available
Right arrow Print PDF (6002K) Freely available
Right arrow Screen PDF (383K) Freely available
Right arrow Supplementary Material
Right arrowOA All Versions of this Article:
35/8/2463    most recent
gkm075v1
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 (7)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Guan, X.
Right arrow Articles by Lu, A-L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Guan, X.
Right arrow Articles by Lu, A-L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2007, Vol. 35, No. 8 2463-2472
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

The human checkpoint sensor Rad9–Rad1–Hus1 interacts with and stimulates NEIL1 glycosylase

Xin Guan1, Haibo Bai1, Guoli Shi1, Corey A. Theriot2, Tapas K. Hazra2, Sankar Mitra2 and A-Lien Lu1,*

1Department of Biochemistry and Molecular Biology and Greenebaum Cancer Center, School of Medicine, University of Maryland, Baltimore, MD 21201, USA and 2Sealy Center for Molecular Medicine and Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX 77555, USA

*To whom correspondence should be addressed. Tel: +1-410-706-4356; Fax: +1-410-706-1787; Email: aluchang{at}umaryland.edu

Received December 14, 2006. Revised January 25, 2007. Accepted January 25, 2007.

The checkpoint protein Rad9/Rad1/Hus1 heterotrimer (the 9-1-1 complex) is structurally similar to the proliferating cell nuclear antigen sliding clamp and has been proposed to sense DNA damage that leads to cell cycle arrest or apoptosis. Human (h) NEIL1 DNA glycosylase, an ortholog of bacterial Nei/Fpg, is involved in repairing oxidatively damaged DNA bases. In this study, we show that hNEIL1 interacts with hRad9, hRad1 and hHus1 as individual proteins and as a complex. Residues 290–350 of hNEIL1 are important for the 9-1-1 association. A significant fraction of the hNEIL1 nuclear foci co-localize with hRad9 foci in hydrogen peroxide treated cells. Human NEIL1 DNA glycosylase activity is significantly stimulated by hHus1, hRad1, hRad9 separately and the 9-1-1 complex. Thus, the 9-1-1 complex at the lesion sites serves as both a damage sensor to activate checkpoint control and a component of base excision repair.


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
 Nucleic Acids ResHome page
W. He, Y. Zhao, C. Zhang, L. An, Z. Hu, Y. Liu, L. Han, L. Bi, Z. Xie, P. Xue, et al.
Rad9 plays an important role in DNA mismatch repair through physical interaction with MLH1
Nucleic Acids Res., October 8, 2008; (2008) gkn686v1.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. L. Hegde, C. A. Theriot, A. Das, P. M. Hegde, Z. Guo, R. K. Gary, T. K. Hazra, B. Shen, and S. Mitra
Physical and Functional Interaction between Human Oxidized Base-specific DNA Glycosylase NEIL1 and Flap Endonuclease 1
J. Biol. Chem., October 3, 2008; 283(40): 27028 - 27037.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
A. Saberi, M. Nakahara, J. E. Sale, K. Kikuchi, H. Arakawa, J.-M. Buerstedde, K. Yamamoto, S. Takeda, and E. Sonoda
The 9-1-1 DNA Clamp Is Required for Immunoglobulin Gene Conversion
Mol. Cell. Biol., October 1, 2008; 28(19): 6113 - 6122.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
Z. Hu, Y. Liu, C. Zhang, Y. Zhao, W. He, L. Han, L. Yang, K. M. Hopkins, X. Yang, H. B. Lieberman, et al.
Targeted Deletion of Rad9 in Mouse Skin Keratinocytes Enhances Genotoxin-Induced Tumor Development
Cancer Res., July 15, 2008; 68(14): 5552 - 5561.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Dou, C. A. Theriot, A. Das, M. L. Hegde, Y. Matsumoto, I. Boldogh, T. K. Hazra, K. K. Bhakat, and S. Mitra
Interaction of the Human DNA Glycosylase NEIL1 with Proliferating Cell Nuclear Antigen: THE POTENTIAL FOR REPLICATION-ASSOCIATED REPAIR OF OXIDIZED BASES IN MAMMALIAN GENOMES
J. Biol. Chem., February 8, 2008; 283(6): 3130 - 3140.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
X. Guan, A. Madabushi, D.-Y. Chang, M. E. Fitzgerald, G. Shi, A. C. Drohat, and A-L. Lu
The human checkpoint sensor Rad9 Rad1 Hus1 interacts with and stimulates DNA repair enzyme TDG glycosylase
Nucleic Acids Res., September 25, 2007; 35(18): 6207 - 6218.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Das, I. Boldogh, J. W. Lee, J. A. Harrigan, M. L. Hegde, J. Piotrowski, N. de Souza Pinto, W. Ramos, M. M. Greenberg, T. K. Hazra, et al.
The Human Werner Syndrome Protein Stimulates Repair of Oxidative DNA Base Damage by the DNA Glycosylase NEIL1
J. Biol. Chem., September 7, 2007; 282(36): 26591 - 26602.
[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.