Abstract

The long-range efforts of this laboratory are directed towards understanding the molecular mechanisms involved in the repair of ionizing radiation damage. To do this we are using a variety of approaches utilizing organisms amenable to both genetic and biochemical techniques. To examine presumptive excision repair of base damage, we have and shall continue to utilize the genetically well characterized organisms, Escherichia coli and Saccharomyces cerevisiae, to attempt to identify enzymes that recognize x-irradiated DNA substrates and to assign particular genes to the enzymes involved. For post replication repair studies, the recombinational repair-deficient bacteriophage T4 mutants, x, y and w are being examined for their particular deficiencies. Further, we are cloning the y and w genes so that we can amplify their products for purification. Lastly, to quantify ionizing radiation damage to DNA so that we may more accurately study repair processes, we are utilizing PM2 bacteriophage and PM2 transfecting DNA as a model system.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
5R01CA033657-05
Application #
3171468
Study Section
Radiation Study Section (RAD)
Project Start
1982-04-01
Project End
1987-01-31
Budget Start
1986-02-01
Budget End
1987-01-31
Support Year
5
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
New York Medical College
Department
Type
Schools of Medicine
DUNS #
City
Valhalla
State
NY
Country
United States
Zip Code
10595

  Publications

Robey-Bond, Susan M; Benson, Meredith A; Barrantes-Reynolds, Ramiro et al. (2017) Probing the activity of NTHL1 orthologs by targeting conserved amino acid residues. DNA Repair (Amst) 53:43-51
Wallace, Susan S; Murphy, Drew L; Sweasy, Joann B (2012) Base excision repair and cancer. Cancer Lett 327:73-89
Faucher, Frederick; Wallace, Susan S; Doublie, Sylvie (2010) The C-terminal lysine of Ogg2 DNA glycosylases is a major molecular determinant for guanine/8-oxoguanine distinction. J Mol Biol 397:46-56
Faucher, Frédérick; Robey-Bond, Susan M; Wallace, Susan S et al. (2009) Structural characterization of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase in its apo form and in complex with 8-oxodeoxyguanosine. J Mol Biol 387:669-79
Faucher, Frédérick; Wallace, Susan S; Doublié, Sylvie (2009) Structural basis for the lack of opposite base specificity of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase. DNA Repair (Amst) 8:1283-9
Faucher, Frédérick; Duclos, Stéphanie; Bandaru, Viswanath et al. (2009) Crystal structures of two archaeal 8-oxoguanine DNA glycosylases provide structural insight into guanine/8-oxoguanine distinction. Structure 17:703-12
Robey-Bond, Susan M; Barrantes-Reynolds, Ramiro; Bond, Jeffrey P et al. (2008) Clostridium acetobutylicum 8-oxoguanine DNA glycosylase (Ogg) differs from eukaryotic Oggs with respect to opposite base discrimination. Biochemistry 47:7626-36
Bandaru, Viswanath; Blaisdell, Jeffrey O; Wallace, Susan S (2006) Oxidative DNA glycosylases: recipes from cloning to characterization. Methods Enzymol 408:15-33
Watanabe, Takashi; Blaisdell, Jeffrey O; Wallace, Susan S et al. (2005) Engineering functional changes in Escherichia coli endonuclease III based on phylogenetic and structural analyses. J Biol Chem 280:34378-84
Blaisdell, J O; Harrison, L; Wallace, S S (2001) Base excision repair processing of radiation-induced clustered DNA lesions. Radiat Prot Dosimetry 97:25-31

Showing the most recent 10 out of 36 publications