Laurey Steinke

Assistant Professor, Biochemistry and Molecular Biology, and Director, Protein Structure Core Facility 

Laurey SteinkePhone: 402-559-5176 
Fax: 402-559-6646

Ph.D., University of Nebraska-Lincoln, 1987

View the Protein Structure Core Facility homepage.


Meta-proteomics of microbial communities and gut microbiome.

Primary Research/Clinical Interests/Expertise:

Environmental proteomics of extremophilic microbes, quantitative proteomics, gut microbiome, determination of sites of protein phosphorylation and enzyme kinetics.

Investigation of Microbial Communities using Proteomic Techniques

Microbes “in the wild” live in communities, unlike the isolated bacteria grown in laboratories. These communities are comprised of various species, most of which have not been isolated. One well-studied community exists as mats of heat loving organisms in Octopus Spring, Yellowstone National Park. One of the major organisms (Synnechococcus) is photosynthetic, and there is evidence that it feeds the other major organism (Roseiflexus). Thus, changes in light throughout the day affect what these bacteria are doing. In addition to the changes in light, the hot spring changes in temperature. Little is known about how microorganisms in a community setting adapt and change in reaction to changes in their surroundings, thus the goal of this research is to investigate this process. The hypothesis driving this work is that the presence of particular proteins will reflect the activities, distribution, and changes in the inhabitants of the microbial mat community during changes in light and temperature. Mass Spectrometry will be used to identify these proteins. The process is called environmental proteomics, signifying that all of the proteins in a sample from the environment will be identified. Genomic and transcriptomic data will be compared to protein data, all collected under the same conditions. In this way, the playbook of the bacteria (the genome) and the planned play (the transcriptome or RNA) can be compared to the actual action on the field—the proteins produced. This methodology is a new approach to identifying the influences of the environment on a microbial community. There is currently much genomic information about the different strains of heat-loving microbes, but characterization of the proteins produced by these organisms is just beginning. Knowledge of the proteins produced by the microorganisms in a well-characterized microbial mat will provide a valuable resource to the microbiological community and will aid in interpreting the microbial fossil record. Proteomic data collected during the course of this project will be deposited in Yellowstone National Park databases. This will coordinate findings from this proposal with the ongoing genomic work in the park. Techniques used to elucidate the protein expression for the well-studied mat communities of Yellowstone, and the procedures determined to be useful in the new field of environmental proteomics will be applicable to microbial communities from other environments, and information gained about community adaptation to changing circumstances may serve as a prototype for microbial communities in other environments.

Other interests:  I am passionate about public science literacy, and participate in community groups supporting this cause. 


Thiel, V., T.L. Hamilton, L.P. Tomsho, R. Burhans, S.E. Gay, R.F. Ramaley,  S.C. Schuster, L. Steinke, and D.A. Bryant.  Draft genome sequence of the moderately thermophilic bacterium Schleiferia thermophila strain Yellowstone (Bacteroidetes). genomeA:   In Press (2014)

Slysz, G.W., L. Steinke, D.M. Ward, C.G. Klatt, T.R.W. Clauss, S.O. Purvine, G.A. Anderson, M.S. Lipton and R.D. Smith. Automated data extraction from in situ protein stable isotope probing studies. J. Proteome Res7, 1200-1210 (2014) DOI: 10.1021/pr400633j  (2014) PMID: 24467184

 Schaffert, C. S., Klatt, C.G., Ward, D.M., Pauley, M. A. and L. Steinke. Identification and distribution of high abundance proteins in an Octopus Spring microbial mat community. Applied and Environmental Microbiology:  78, 8481-8484 (2012). PMC3497366

 Joseph, P., Suman, S.P., Li, S., Fontaine, M. and L. Steinke.  Amino acid sequence of myoglobin from white-tailed deer (Odocoileus virginianus).  Meat Science 92, 160-163 (2012). PMID: 22608832

 Suman,  S.P., Joseph, P.,  Li, S.,  Fontaine, M. and L. Steinke.  Primary structure of turkey myoglobin.  Food Chemistry:  129: 175-178 (2011).

 Suman,  S.P., Joseph, P.,  Li, S.,  Steinke, L., and M. Fontaine. Amino acid sequence of myoglobin from emu (Dromaius novaehollandiae) skeletal muscle.  Meat Science 86, 623-628 (2010). PMID: 20621424

 Joseph, P., Suman,  S.P.,  Li, S.,  Beach, C.M., Steinke, L., and M. Fontaine  Characterization of bison (Bison bison) myoglobin.  Meat Science 84, 71-78 (2010). PMID: 20374756

 Suman,  S.P., Joseph, P.,  Li, S.,  Steinke, L., and M. Fontaine  Primary structure of goat myoglobin.  Meat Science 82, 456-460 (2009). PMID: 20416681

 Brune, D., Crawford, J.M., Cook, R.G., Denslow, N.D., Kobayashi, R., Madden, B.J., Neveu, J.M., and L. Steinke ABRF ESRG 2004 Study:  Modified Amino Acids in Edman Sequencing. Journal of Biomolecular Techniques 16, 272-284 (2005). PMC2291730

 Buckel., S.D., Cook, R.G., Crawford, J.M., Dupont, D.R., Madden, B.J., Neveu, J.M., Steinke, L., and J. Fernandez.  ABRF-2002ESRG, a Difficult Sequence:  Analysis of a PVDF-Bound Known Protein with a Heterogeneous Amino Terminus. Journal of Biomolecular Techniques 13, 246-257 (2002). PMC2279867

Henzel, W.J., Admon, A., Carr, S.A., Davis, G., DeJongh, K., Lane, W., Rohde, M., and L. Steinke.  ABRF-98SEQ:  Evaluation of Peptide Sequencing at High Sensitivity. . Journal of Biomolecular Techniques 11, 92-99 (2000). PMC2291621

 Volle, D.J. Fulton, J.A., Chaika, O.V., Huang, H., McDermott, K., Steinke, L. and Lewis R.E.  Phosphorylation of Kinase Suppressor of Ras by Associated Kinases.  Biochemistry  38, 5130-5137  (1999). PMID: 10213618

 Stone,  K.; Fernandez, J.;   Admon, A.;  Henzel, W.;  Lane, W.;  Rohde, M.; and Steinke,   L.  ABRF-97SEQ:  Sequencing results of a low level sample. Journal of Biomolecular    Techniques  10, 26-32 (1999).   PMC: 2291579

DeBoer, L.W.V., Bekx, P.A., Han, L. and L. Steinke. Pyruvate enhances recovery of "stunned myocardium" in isolated rat hearts by preventing free radical generation. Am. J. Physiol.  265, H1571-1576 (1993). PMID: 8238569

Nair*, B. G., Steinke*, L.; Yu, Y.; Rashed, H. M.; Seyer, H.; and Patel, T. Increase in the Number of Atrial Natriuretic Hormone Receptors in Regenerating Rat Liver  J. Biol. Chem. 266, 567-573 (1991). (*co-first authors) PMID: 1670770

 Steinke, L., Bacon, R. and Schuster, S.M. The Effects of Exchange-inert Metal Nucleotide Complexes on the Kinetics of Beef Heart Mitochondrial ATPase Arch. Biochem. and Biophys., 238, 482-490 (1987). PMID: 2890328

 Steinke, L. and Schuster, S.M. The Effect of Co(III)(NH3)4ATP on the Kinetics of Beef Heart Mitochondrial ATPase  Arch. Biochem. and Biophys., 238, 629-635 (1985). PMID: 2859840

Chapters in Books:

Steinke, L. and R.G. Cook. "Identification of Phosphorylation Sites by Edman Degradation" in Protein Sequencing Protocols. B.J. Smith, Humana Press, Totawa, NJ, pp. 301-308, 2003.

Grant Support:

National Science Foundation
Elucidation of Microbial Response to Temperature Variation and the Diurnal Cycle in the Yellowstone Octopus Hot Spring: A Proteomic Study
9/1/2008 - 8/31/2012

Department of Energy
Foundational Scientific Focus Area: Microbial Interactions
10/1/2010 - 9/30/2014