Natural Sciences Faculty

Aaron Setterdahl

Assistant Professor of Chemistry

Education

  • Post-doctoral fellow, Indiana University, Bloomington, IN, 2007
  • Japanese Society for the Promotion of Science Fellowship, Osaka University, Japan. 2003
  • Ph.D. Biochemistry, Texas Tech University, Lubbock, TX, 2001
  • B.S. Chemistry, Iowa State University, Ames IA, 1997

Publications

  1. Bauer, C. E., Setterdahl, A., Wu, J., and Robinson, B. R. (2009) Regulation of Gene Expression in Response to Oxygen Tension, In The Purple Phototrophic Bacteria (Advances in Photosynthesis and Respiration) (Hunter, C. N., Daldal, F., Thurnauer, M. C., and Beatty, J. T., Eds.), pp 707-725, Springer.
  2. Tripathy, J. N., Hirasawa, M., Kim, S. K., Setterdahl, A. T., Allen, J. P., and Knaff, D. B. (2007) The role of tryptophan in the ferredoxin-dependent nitrite reductase of spinach, Photosynth Res 94, 1-12. http://www.ncbi.nlm.nih.gov/pubmed/17611813
  3. Kim, S. K., Mason, J. T., Knaff, D. B., Bauer, C. E., and Setterdahl, A. T. (2006) Redox properties of the Rhodobacter sphaeroides transcriptional regulatory proteins PpsR and AppA, Photosynth Res 89, 89-98. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2774731
  4. Swem, D. L., Swem, L. R., Setterdahl, A., and Bauer, C. E. (2005) Involvement of SenC in assembly of cytochrome c oxidase in Rhodobacter capsulatus, J Bacteriol 187, 8081-8087. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1291261
  5. Brehelin, C., Laloi, C., Setterdahl, A. T., Knaff, D. B., and Meyer, Y. (2004) Cytosolic, mitochondrial thioredoxins and thioredoxin reductases in Arabidopsis thaliana, Photosynth Res 79, 295-304. http://www.ncbi.nlm.nih.gov/pubmed/16328796
  6. Swem, L. R., Kraft, B. J., Swem, D. L., Setterdahl, A. T., Masuda, S., Knaff, D. B., Zaleski, J. M., and Bauer, C. E. (2003) Signal transduction by the global regulator RegB is mediated by a redox-active cysteine, EMBO J 22, 4699-4708. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC212728
  7. Setterdahl, A. T., Chivers, P. T., Hirasawa, M., Lemaire, S. D., Keryer, E., Miginiac-Maslow, M., Kim, S. K., Mason, J., Jacquot, J. P., Longbine, C. C., de Lamotte-Guery, F., and Knaff, D. B. (2003) Effect of pH on the oxidation-reduction properties of thioredoxins, Biochemistry 42, 14877-14884. http://www.ncbi.nlm.nih.gov/pubmed/14674763
  8. Masuda, S., Dong, C., Swem, D., Setterdahl, A. T., Knaff, D. B., and Bauer, C. E. (2002) Repression of photosynthesis gene expression by formation of a disulfide bond in CrtJ, Proc Natl Acad Sci U S A 99, 7078-7083. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC124531
  9. Bick, J. A., Setterdahl, A. T., Knaff, D. B., Chen, Y., Pitcher, L. H., Zilinskas, B. A., and Leustek, T. (2001) Regulation of the plant-type 5'-adenylyl sulfate reductase by oxidative stress, Biochemistry 40, 9040-9048. http://www.ncbi.nlm.nih.gov/pubmed/11467967
  10. Setterdahl, A. T., Goldman, B. S., Hirasawa, M., Jacquot, P., Smith, A. J., Kranz, R. G., and Knaff, D. B. (2000) Oxidation-reduction properties of disulfide-containing proteins of the Rhodobacter capsulatus cytochrome c biogenesis system, Biochemistry 39, 10172-10176. http://www.ncbi.nlm.nih.gov/pubmed/10956006
  11. Setterdahl, A., Hirasawa, M., Bucher, L. M., Dholakia, C. A., Jacquot, P., Yards, H., Miller, F., Stevens, F. J., Knaff, D. B., and Anderson, L. E. (2000) Oxidation-reduction properties of two engineered redox-sensitive mutant Escherichia coli malate dehydrogenases, Arch Biochem Biophys 382, 15-21. http://www.ncbi.nlm.nih.gov/pubmed/11051092
  12. Yokota, Y., Jacobson, R. A., Logsdon, B. C., Ringrose, S., Setterdahl, A. T., and Verkade, J. G. (1999) Synthesis of alkali and alkaline earth metal complexes of open cryptands and their X-ray structures wherein M=Li+, Na+ and Ba2+, Polyhedron 18.

Research Interests

The diversity of organisms on Earth is largely determined by the differences in genes that they contain in their genome. Even with the apparent diversity outwardly displayed by all organisms, there are significant numbers of genes that are shared throughout. Genome sequencing of thousands of organisms in recent years has revealed an enormous database of gene sequences that code for many previously unknown proteins. From humans to plants to fungi and bacteria, a large proportion of the genes encoded with in these organisms have no known function. The goal of this research is to identify genes in the purple photosynthetic bacterium Rhodobacter sphaeroides, clone these genes, express and purify the proteins that are encoded in these genes, and then characterize the functions of the purified proteins. Knowledge of the function of these genes will give significant insight which may allow for engineering of the bacteria for clean energy, or identify new functions which would be used in unforeseen medical, environmental or engineering applications.

R. sphaeroides is a purple photosynthetic bacterium that has been well-studied for many years. The Rhodobacter species growth modes include aerobic and anaerobic respiration, anaerobic photosynthesis, fermentation, use of diverse organic carbon sources, or use of carbon dioxide (CO2) as the sole carbon source both aerobically and anaerobically. Purple photosynthetic bacteria have been isolated from a variety of soils, plants, and aqueous environments ranging from fresh water to salt water and temperatures from hot springs to polar ice caps. Because the physiology of R. sphaeroides is well known, this makes it an ideal candidate for a gene knockout study because observation of different physiological phenotypes would allow the function of the deleted gene to be elucidated.

Sequence analysis of a purple photosynthetic bacterium R. sphaeroides reveals several protein sequences that are uncharacterized and are highly conserved among bacteria such as Escherichia coli, Staphylococcus aureus, Xanthomonas axonopodis, Bradyrhizobium japonicum, Rhodopirellula baltica, Gluconobacter oxydans, Pseudomonas syringae, Shigella sonnei, Tenacibaculum, Flavobacterium, Blastopirellula marina, Rickettsiella grylli, Mesorhizobium, Streptomyces ambofaciens, Enterobacter spp., Planctomyces maris, and Klebsiella pneumoniae. The primary objectives of the project are to clone the genes encoding several highly conserved proteins and to express and purify the proteins of which the genes encode, and characterize the biochemical properties of the proteins.

Genomic sequences are just the beginning of our understanding of how organisms work. Even with detailed annotation of genomes in which sequences of DNA from one organism are compared to other DNA sequences of different organisms, not all genes and their respective gene products can be correctly identified. In fact, numerous instances exist where annotation reveals many genes to be "unknown function" or "hypothetical protein." This is why individual gene study is a necessary and potentially rewarding process in which new previously unidentified functions will be discovered for the first time.

Teaching Areas

CHEM C102 ELEMENTARY CHEMISTRY 2

CHEM C122 ELEMENTARY CHEMISTRY 2 LABORATORY

CHEM C484 BIOMOLECULES AND CATABOLISM

CHEM C485 BIOSYNTHESIS AND PHYSIOLOGY

CHEM C486 BIOLOGICAL CHEMISTRY LABORATORY