My research group is focused on defining the biochemical mechanisms involved in the perception of and protection against oxidative stress and other toxic compounds using the model organism, Saccharomyces cerevisiae. Oxidative stress is caused by increased levels of reactive oxygen species such as superoxide anion, hydrogen peroxide and hydroxyl radicals and has been implicated in several degenerative diseases and the aging process. Reactive oxygen species can result from incomplete reduction of molecular oxygen and exposure to radiation or toxic chemicals found in the environment. To defend against oxidative stress, organisms have evolved specific signal transduction pathways that regulate the transcription of genes involved in detoxification and protection against reactive oxygen species. By defining the molecular mechanisms by which oxidative and environmental stresses alter cellular signaling pathways and gene expression, my research group hopes to develop new technologies for monitoring and remediation of oxidative stress and environmental toxicants. In line with the broad scope of my laboratory, we use a variety of approaches to characterize the structure and function of proteins as well as cell and molecular biology, yeast genetics and genome-wide approaches.
- Postdoctoral Associate, National Institutes of Health, 2001-2005
- Ph.D. Biochemistry, University of California, San Diego, 2000
- B.S. Biochemistry, University of California, San Diego, 1997 M.S.
- Chemistry, University of California, Santa Cruz, 1996 B.S.
- ETX 220 - Analysis of Toxicants
- ETX 220L - Analysis of Toxicants Laboratory
- Director of the Wood Laboratory
- Member of the Agricultural and Environmental Chemistry Graduate Group
- Member of the Pharmacology and Toxicology Graduate Group
- Member of the Biochemistry and Molecular Biology Graduate Group
- Member of the Cell and Developmental Biology Graduate Group
Mason, J.T., Kim, S.K., Knaff, D.B. & Wood, M.J. (2006) Thermodynamic basis for redox regulation of the Yap1 signal transduction pathway. Biochemistry, 45, 13409-13417.
Wang, X., Mukhopadhyay, P., Wood, M.J., Outten, F.W., Opdyke, J.A., & Storz, G. (2006) Mutational Analysis to Define an Activating Region on the Redox-Sensitive Transcriptional Regulator OxyR. Journal of Bacteriology, 188, 8335-8342.
Prieto, J.H., Sampoli Benitez, B.A., Melacini, G., Johnson, D.A., Wood, M.J. & Komives E.A. (2005) Dynamics of the Fragment of Thrombomodulin containing the fourth and fifth EGF-like domains correlate with function. Biochemistry, 44, 1225-1233.
Wood, M.J., Storz, G. & Tjandra, N. (2004) Structural basis for redox regulation of Yap1 transcription factor localization. Nature, 430, 917-921.
Wood, M.J., Andrade, E.C. & Storz, G. (2003) The redox domain of the Yap1p transcription factor contains two disulfide bonds. Biochemistry, 42, 11982-11991.
Outten, F.W., Wood, M.J., Munoz, F.M. & Storz, G. (2003) The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. Journal of Biological Chemistry, 278, 45713-9.
Wood, M.J., Becvar, L.A., Prieto, J.H., Melacini, G. & Komives, E.A. (2003) NMR structures reveal how oxidation inactivates thrombomodulin. Biochemistry, 42, 11932-11942.