Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (284K) 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 (12)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Moe, A.
Right arrow Articles by Klungland, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moe, A.
Right arrow Articles by Klungland, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2003, Vol. 31, No. 14 3893-3900
© 2003 Oxford University Press

Incision at hypoxanthine residues in DNA by a mammalian homologue of the Escherichia coli antimutator enzyme endonuclease V

Ane Moe, Jeanette Ringvoll, Line M. Nordstrand, Lars Eide, Magnar Bjørås, Erling Seeberg, Torbjørn Rognes and Arne Klungland*

Centre for Molecular Biology and Neuroscience and Institute of Medical Microbiology, University of Oslo, Rikshospitalet, N-0027 Oslo, Norway

*To whom correspondence should be addressed. Tel: +47 23074069; Fax: +47 23074061; Email: arne.klungland{at}labmed.uio.no

Deamination of DNA bases can occur spontaneously, generating highly mutagenic lesions such as uracil and hypoxanthine. In Escherichia coli two enzymes initiate repair at hypoxanthine residues in DNA. The alkylbase DNA glycosylase, AlkA, initiates repair by removal of the damaged base, whereas endonuclease V, Endo V, hydrolyses the second phosphodiester bond 3' to the lesion. We have identified and characterised a mouse cDNA with striking homology to the E.coli nfi gene, which also has significant similarities to motifs required for catalytic activity of the UvrC endonuclease. The 37-kDa mouse enzyme (mEndo V) incises the DNA strand at the second phosphodiester bond 3' to hypoxanthine- and uracil-containing nucleotides. The activity of mEndo V is elevated on single-stranded DNA substrate in vitro. Expression of the mouse protein in a DNA repair-deficient E.coli alkA nfi strain suppresses its spontaneous mutator phenotype. We suggest that mEndo V initiates an alternative excision repair pathway for hypoxanthine removal. It thus appears that mEndo V has properties overlapping the function of alkylbase DNA glycosylase (Aag) in repair of deaminated adenine, which to some extent could explain the absence of phenotypic abnormalities associated with Aag knockout in mice.


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
J. L. Parsons, B. D. Preston, T. R. O'Connor, and G. L. Dianov
DNA polymerase {delta}-dependent repair of DNA single strand breaks containing 3'-end proximal lesions
Nucleic Acids Res., February 28, 2007; 35(4): 1054 - 1063.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
T. Nakano, A. Katafuchi, R. Shimizu, H. Terato, T. Suzuki, H. Tauchi, K. Makino, M. Skorvaga, B. Van Houten, and H. Ide
Repair activity of base and nucleotide excision repair enzymes for guanine lesions induced by nitrosative stress
Nucleic Acids Res., April 14, 2005; 33(7): 2181 - 2191.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
S. Kanugula, G. T. Pauly, R. C. Moschel, and A. E. Pegg
A bifunctional DNA repair protein from Ferroplasma acidarmanus exhibits O6-alkylguanine-DNA alkyltransferase and endonuclease V activities
PNAS, March 8, 2005; 102(10): 3617 - 3622.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
H. Pincas, M. R. Pingle, J. Huang, K. Lao, P. B. Paty, A. M. Friedman, and F. Barany
High sensitivity EndoV mutation scanning through real-time ligase proofreading
Nucleic Acids Res., October 28, 2004; 32(19): e148 - e148.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
T. M. Hitchcock, H. Gao, and W. Cao
Cleavage of deoxyoxanosine-containing oligodeoxyribonucleotides by bacterial endonuclease V
Nucleic Acids Res., August 2, 2004; 32(13): 4071 - 4080.
[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.