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Volume 270, Number 2, Issue of January 13, 1995 pp. 949-957
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
DNA Polymerase Conducts the Gap-filling Step in Uracil-initiated Base Excision Repair in a Bovine Testis Nuclear Extract

(Received for publication, August 5, 1994; and in revised form, October 26, 1994)

Rakesh K. Singhal ,  Rajendra Prasad,  Samuel H. Wilson

The G:U mismatch in genomic DNA mainly arises from deamination of cytosine residues and is repaired by the base excision repair pathway. We found that a bovine testis crude nuclear extract conducts uracil-initiated base excision repair in vitro. A 51-base pair synthetic DNA substrate containing a single G:U mismatch was used, and incorporation of dCMP during repair was exclusively to replace uracil. A neutralizing polyclonal antibody against DNA polymerase beta (beta-pol) inhibited the repair reaction. ddCTP also inhibited the repair reaction, whereas aphidicolin had no significant effect, suggesting that activity of beta-pol was required. Next, the base excision repair system was reconstituted using partially purified components. Several of the enzymatic activities required were resolved, such that DNA ligase and the uracil-DNA glycosylase/apurinic/apyrimidinic endonuclease activities were separated from the DNA polymerase requirement. We found that purified beta-pol could restore full DNA repair activity to the DNA polymerase-depleted fraction, whereas purified DNA polymerases alpha, , and could not. These results with purified proteins corroborated results obtained with the crude extract and indicate that beta-pol is responsible for the single-nucleotide gap filling reaction involved in this in vitro base excision repair system.



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J. Biol. Chem., July 5, 1996; 271(27): 16000 - 16007.
[Abstract] [Full Text] [PDF]

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N. Oda, J. K. Saxena, T. M. Jenkins, R. Prasad, S. H. Wilson, and E. J. Ackerman
DNA Polymerases alpha and beta Are Required for DNA Repair in an Efficient Nuclear Extract from Xenopus Oocytes
J. Biol. Chem., June 7, 1996; 271(23): 13816 - 13820.
[Abstract] [Full Text] [PDF]

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W. A. Beard, W. P. Osheroff, R. Prasad, M. R. Sawaya, M. Jaju, T. G. Wood, J. Kraut, T. A. Kunkel, and S. H. Wilson
Enzyme-DNA Interactions Required for Efficient Nucleotide Incorporation and Discrimination in Human DNA Polymerase beta
J. Biol. Chem., May 24, 1996; 271(21): 12141 - 12144.
[Abstract] [Full Text] [PDF]

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G. Frosina, P. Fortini, O. Rossi, F. Carrozzino, G. Raspaglio, L. S. Cox, D. P. Lane, A. Abbondandolo, and E. Dogliotti
Two Pathways for Base Excision Repair in Mammalian Cells
J. Biol. Chem., April 19, 1996; 271(16): 9573 - 9578.
[Abstract] [Full Text] [PDF]

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Y Matsumoto and K Kim
Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair
Science, August 4, 1995; 269(5224): 699 - 702.
[Abstract] [PDF]

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D. K. Srivastava, T. Y. Rawson, S. D. Showalter, and S. H. Wilson
Phorbol Ester Abrogates Up-regulation of DNA Polymerase [IMAGE] by DNA-alkylating Agents in Chinese Hamster Ovary Cells
J. Biol. Chem., July 7, 1995; 270(27): 16402 - 16408.
[Abstract] [Full Text] [PDF]

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M. J. Jezewska, S. Rajendran, and W. Bujalowski
Energetics and Specificity of Rat DNA Polymerase beta Interactions with Template-primer and Gapped DNA Substrates
J. Biol. Chem., May 4, 2001; 276(19): 16123 - 16136.
[Abstract] [Full Text] [PDF]

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O. I. Lavrik, R. Prasad, R. W. Sobol, J. K. Horton, E. J. Ackerman, and S. H. Wilson
Photoaffinity Labeling of Mouse Fibroblast Enzymes by a Base Excision Repair Intermediate. EVIDENCE FOR THE ROLE OF POLY(ADP-RIBOSE) POLYMERASE-1 IN DNA REPAIR
J. Biol. Chem., June 29, 2001; 276(27): 25541 - 25548.
[Abstract] [Full Text] [PDF]

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T. A. Ranalli, M. S. DeMott, and R. A. Bambara
Mechanism Underlying Replication Protein A Stimulation of DNA Ligase I
J. Biol. Chem., January 11, 2002; 277(3): 1719 - 1727.
[Abstract] [Full Text] [PDF]


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