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Department of Biological Science

at Florida State University

Biological Science Faculty Member

Dr. M. Elizabeth Stroupe

  • Office: 202 Kasha Laboratory
  • Office: (850) 644-1751
  • Lab: 218 Kasha Laboratory Building
  • Lab: (850) 645-9317
  • Fax: (850) 644-2259
  • Mail code: 4380
  • E-mail: mestroupe@bio.fsu.edu
Dr. M. Elizabeth Stroupe

Laboratory Home Page

Associate Professor
Ph.D., Scripps Research Institute, 2002
Graduate Faculty Status

 





Research and Professional Interests:

What is the relationship between a molecule's structure and its activity in the cell? I am interested in understanding the structure/function relationships driving two pathways: the transformation of a gene into a protein and sulfur metabolism. The two projects in my laboratory are not related topically, but are united in approach. Questions that interest me about the progression of information from a gene to a protein include: how is gene expression controlled by alternative DNA structures? How are ribosomes assembled into functional units? Questions that interest me about the biochemical basis for sulfur metabolism include: how do electrons move from the reductase subunit to the active site of the central sulfur metabolic enzyme sulfite reductase? How is sulfite reductase' essential metallic cofactor synthesized? I use x-ray crystallography and single-particle cryogenic electron microscopy (cryo-EM) to probe across resolutions so I can link atomic resolution details, macromolecular assemblies, and cellular activity.

The lab uses a combination of x-ray crystallography and cryo-EM to determine the structure and function of these important biomolecules.

Selected Publications:

Johnson, M. C.*,Ghalei, H.*, Doxtader, K. A., Karbstein, K., & Stroupe, M. E. (in press.) Structural Heterogeneity in Pre-40S Ribosomes.

 

Khoshnevis, S., Askenasy, I., Johnson, M. C., Dattolo, M. D., Young-Erdos, C. L., Stroupe, M. E., & Karbstein, K. (2016.) The DEAD-box Protein Rok1 Orchestrates 40S and 60S Ribosome Assembly by Promoting the Release of Rrp5 from Pre-40S Ribosomes to Allow for 60S Maturation. PLoS Biology. Retrieved from: http://journals.plos.org/plosbiology/article?id=10.1371/journal.pbio.1002480 doi:10.1371/journal.pbio.1002480

Johnson, M. C., Tatum, K. B., Lynn, J. S., Brewer, T. E., Washburn, B. K., Stroupe, M. E., & Jones, K. M. (2015). Sinorhizobium meliloti phage ΦM9 defines a new group of T4-superfamily phages with unusual genomic features, but a common T=16 capsid. Journal of Virology, 10945-10958. Retrieved from http://jvi.asm.org/content/89/21/10945.long doi:10.1128/JVI.01353-15

Askenasy, I., Pennington, J. M., Tao, Y., Marshall, A. G., Young, N. L., Sheng, W., & Stroupe, M. E. (2015). The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain that Mediates Holoenzyme Assembly. Journal of Biological Chemistry, 290, 15. Retrieved from http://www.jbc.org/content/early/2015/06/18/jbc.M115.662379.full.pdf+html doi:10.1074/jbc.M115.662379

Ghalei, H., Schaub, F., Doherty, J., Roush, W. R., Cleveland, J. J., Stroupe, M. E., & Karbstein, K. (2015). Hrr25/CK1δ-directed release of Ltv1 from pre-40S ribosomes is necessary for ribosome assembly and cell growth. The Journal of Cell Biology, 208, 745-759. Retrieved from http://jcb.rupress.org/content/208/6/745.full.pdf+html doi:10.1083/jcb.201409056

Kopylov, M., Bass, H. W., & Stroupe, M. E. (2015). Identification and characterization of a plant G-quadruplex-binding protein encoded by the maize (Zea mays L.) nucleoside diphosphate kinase1 gene, ZmNDPK1. Biochemistry, 54, 1743-1757. Retrieved from http://pubs.acs.org/doi/abs/10.1021/bi501284g doi:10.1021/bi501284g

Andorf, C. M., Kopylov, M., Dobbs, D., Koch, K. E., Stroupe, M. E., Lawrence, C. J., & Bass, H. W. (2014). G-Quadruplex (G4) Motifs in the Maize (Zea mays L.) Genome Are Enriched at Specific Locations in Thousands of Genes Coupled to Energy Status, Hypoxia, Low Sugar, and Nutrient Deprivation. J Genet Genomics, 12, 627-647. Retrieved from http://www.sciencedirect.com/science/article/pii/S1673852714001866 doi:10.1016/j.jgg.2014.10.004 

Brewer, T., Stroupe, M. E., & Jones, K. M. (2014). The genome, proteome and phylogenetic analysis of Sinorhizobium meliloti phage ΦM12, the founder of a new group of T4-superfamily phages. Virology, 450-451, 84-97. Retrieved from http://www.sciencedirect.com/science/article/pii/S0042682213006491 doi:10.1016/j.virol.2013.1

Stroupe, M. E., Brewer, T., Sousa, D. R., & Jones, K. M. (2014). The structure of Sinorhizobium meliloti phage ΦM12, which has a novel T=19l triangulation number and is the founder of a new group of T4-superfamily phages. Virology, 450-451, 205-212. Retrieved from http://www.sciencedirect.com/science/article/pii/S0042682213006399 doi:10.1016/j.virol.2013.1

Sousa, D. R., Stagg, S. M., & Stroupe, M. E. (2013). Cryo-EM structures of the actin:tropomyosin filament reveal the mechanism for the transition from C- to M-state. J Mol Biol, 425(22), 4544-55. Retrieved from http://www.sciencedirect.com/science/article/pii/S0022283613005408 doi:10.1016/j.jmb.2013.08.020

Smith, K. W., & Stroupe, M. E. (2012). Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer. Biochemistry, 51(49), 9857-68. Retrieved from http://pubs.acs.org/doi/abs/10.1021/bi300947a doi:10.1021/bi300947a

Postdoctoral Associates:

Rai, Jay

Graduate Students:

Askenasy, Isabel

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