Skip to Content

'
Richard D. Wood, PhD

Present Title & Affiliation

Primary Appointment

Grady F. Saunders Distinguished Professor in Molecular Biology, The University of Texas M. D. Anderson Cancer Center, Smithville, TX

Research Interests

Many enzymes and regulatory proteins are devoted to the repair of DNA damage arising from agents inside cells and from the environment. DNA repair is a front-line defense against the mutations that can accumulate to cause cancer. Research in my laboratory includes exploration of the biochemical mechanism of the DNA nucleotide excision repair pathway in human cells. We have reconstituted the process with purified proteins and can dissect intermediatesin the reaction. In one study we are examining how this repair process participates in resolving cross-links between DNA strands. We also investigate several DNA polymerases that help cells tolerate DNA damage. Some of the work is with a mouse model deficient in DNA polymerase zeta, to understand the role of this enzyme in chromosome instability, skin carcinogenesis and mammary carcinogenesis. In addition, we are determining the biochemical and cellular functions of two other specialized DNA polymerases which were isolated in ourlaboratory, POLQ and POLN. These are nuclear enzymes present only in higher eukaryotes and both have an unusual ability to bypass specific lesions in DNA templates. This research will provide insights into how DNA damage is tolerated in cells before it is repaired.

Education & Training

Degree-Granting Education

1981 University of California, Berkeley, Berkeley, CA, PHD, Biophysics
1977 Westminster College, Salt Lake City, UT, BS, Biology, Mathematics

Postgraduate Training

1985-1988 Research Fellowship, Imperial Cancer Research Fund, Lincoln's Inn Fields, London, United Kingdom
1982-1985 Research Fellowship, Yale University, New Haven, CT

Selected Publications

Peer-Reviewed Original Research Articles

1. Bhagwat NR, Roginskaya VY, Acquafondata MB, Dhir R, Wood RD, Niedernhofer LJ. Immunodetection of DNA repair endonuclease ERCC1-XPF in human tissue. Cancer Res 69(17):6831-8, 9/2009.
2. Goff JP, Shields DS, Seki M, Choi S, Epperly MW, Dixon T, Wang H, Bakkenist CJ, Dertinger SD, Torous DK, Wittschieben J, Wood RD, Greenberger JS. Lack of DNA polymerase theta (POLQ) radiosensitizes bone marrow stromal cells in vitro and increases reticulocyte micronuclei after total-body irradiation. Radiat Res 172(2):165-74, 8/2009.
3. Koberle B, Roginskaya V, Zima KS, Masters JR, Wood RD. Elevation of XPA protein level in testis tumor cells without increasing resistance to cisplatin or UV radiation. Mol Carcinog 47(8):580-6, 8/2008. PMID: 18240296.
4. Gan GN, Wittschieben JP, Wittschieben BØ, Wood RD. DNA polymerase zeta (pol zeta) in higher eukaryotes. Cell Res 18(1):174-83, 1/2008. PMID: 18157155.
5. Arana ME, Takata K, Garcia-Diaz M, Wood RD, Kunkel TA. A unique error signature for human DNA polymerase nu. DNA Repair (Amst) 6(2):213-23, 2/2007. PMCID: PMC1950682.
6. Takata K, Shimizu T, Iwai S, Wood RD. Human DNA polymerase N (POLN) is a low fidelity enzyme capable of error-free bypass of 5S-thymine glycol. J Biol Chem 281(33):23445-55, 8/2006. PMID: 16787914.
7. Köberle B, Roginskaya V, Wood RD. XPA protein as a limiting factor for nucleotide excision repair and UV sensitivity in human cells. DNA Repair (Amst) 5(5):641-8, 5/2006. PMID: 16413230.
8. Wittschieben JP, Reshmi SC, Gollin SM, Wood RD. Loss of DNA polymerase zeta causes chromosomal instability in mammalian cells. Cancer Res 66(1):134-42, 1/2006. PMID: 16397225.
9. Wittschieben BO, Iwai S, Wood RD. DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA. J Biol Chem 280(48):39982-9, 12/2005. PMID: 16223728.
10. Seki M, Masutani C, Yang LW, Schuffert A, Iwai S, Bahar I, Wood RD. High-efficiency bypass of DNA damage by human DNA polymerase Q. EMBO J 23(22):4484-94, 11/2004. PMCID: PMC526458.

Last updated: 10/14/2009