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PMID: 10455196 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Enzymatic repair of 5-formyluracil. II. Mismatch formation between 5-formyluracil and guanine during dna replication and its recognition by two proteins involved in base excision repair (AlkA) and mismatch repair (MutS).

The Journal of biological chemistry ·Vol. 274 ·No. 35 ·1999-08-27 ·Pages 25144-50

Terato H, Masaoka A, Kobayashi M, Fukushima S, Ohyama Y, Yoshida M, Ide H

Abstract

5-Formyluracil (fU), a major methyl oxidation product of thymine, forms correct (fU:A) and incorrect (fU:G) base pairs during DNA replication. In the accompanying paper (Masaoka, A., Terato, H., Kobayashi, M., Honsho, A., Ohyama, Y., and Ide, H. (1999) J. Biol. Chem. 274, 25136-25143), it has been shown that fU correctly paired with A is recognized by AlkA protein (Escherichia coli 3-methyladenine DNA glycosylase II). In the present work, mispairing frequency of fU with G and cellular repair protein that specifically recognized fU:G mispairs were studied using defined oligonucleotide substrates. Mispairing frequency of fU was determined by incorporation of 2'-deoxyribonucleoside 5'-triphosphate of fU opposite template G using DNA polymerase I Klenow fragment deficient in 3'-5' exonuclease. Mispairing frequency of fU was dependent on the nearest neighbor base pair in the primer terminus and 2-12 times higher than that of thymine at pH 7.8 and 2.6-6.7 times higher at pH 9.0 with an exception of the nearest neighbor T(template):A(primer). AlkA catalyzed the excision of fU placed opposite G, as well as A, and the excision efficiencies of fU for fU:G and fU:A pairs were comparable. In addition, MutS protein involved in methyl-directed mismatch repair also recognized fU:G mispairs and bound them with an efficiency comparable to T:G mispairs, but it did not recognize fU:A pairs. Prior complex formation between MutS and a heteroduplex containing an fU:G mispair inhibited the activity of AlkA to fU. These results suggest that fU present in DNA can be restored by two independent repair pathways, i.e. the base excision repair pathway initiated by AlkA and the methyl-directed mismatch repair pathway initiated by MutS. Biological relevance of the present results is discussed in light of DNA replication and repair in cells.

MeSH Terms
Adenine/chemistry Adenosine Triphosphatases Bacterial Proteins/metabolism Base Pair Mismatch/genetics DNA Glycosylases DNA Repair/genetics DNA Replication/genetics DNA-Binding Proteins Escherichia coli Proteins Guanine/chemistry Kinetics MutS DNA Mismatch-Binding Protein N-Glycosyl Hydrolases/metabolism Oligodeoxyribonucleotides/chemistry Thymine/chemistry Uracil/analogs & derivatives,chemistry
Chemicals
Bacterial Proteins DNA-Binding Proteins Escherichia coli Proteins Oligodeoxyribonucleotides 5-formyluracil Uracil Guanine DNA Glycosylases N-Glycosyl Hydrolases DNA-3-methyladenine glycosidase II Adenosine Triphosphatases MutS DNA Mismatch-Binding Protein MutS protein, E coli Adenine Thymine
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Terato H
Graduate Department of Gene Science, Faculty of Science, Hiroshima University, Kagamiyama, Higashi-Hiroshima 739-8526, Japan.
Masaoka A
Kobayashi M
Fukushima S
Ohyama Y
Yoshida M
Ide H
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1999-08-27
Pages
25144-50
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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