Eric R. Schreiter
Assistant Professor of Chemistry, UPR Rio Piedras Campus
Adjunct Professor of Biochemistry, URP Medical Sciences Campus
Contact
Email:
Office:
NCN-230 - Located on the second floor of the Natural Sciences Building
Phone: 787-764-0000 ext. 4796
Laboratory:
NCN-115 and NCN-117 - First floor of the Natural Sciences Building
Phone: 787-764-0000 ext. 2769
Members of the Schreiter Lab.
Education
~ Ph.D. in Biological Chemistry from Massachusetts Institute of Technology (2005)
Advisor: Dr. Catherine L. Drennan
~ Postdoc at Brigham and Women's Hospital/Harvard Medical School
Advisor: Dr. Richard T. Lee
~ Postdoc at University of Puerto Rico Protein Research Center
Research Interests
Biochemistry, Protein structure and function, Post-translational protein modifications, Protein engineering, Unusual metabolic pathways of extremophile bacteriaCurrent Projects
Molecular analysis of protein S-nitrosylation: In this NIH-funded project, we seek to underderstand protein S-nitrosylation at the molecular level. S-nitrosylation, or attachment of a nitric oxide group to the sulfur of a cysteine within a protein, has the ability to modulate protein structure and function and aberrant S-nitrosylation has been linked to several human diseases. Specifically, we are interested in the nature of the specificity observed for this modification as well as exploring the structural and functional consequences of S-nitrosylation in several important protein systems. The figure at right depicts the details of protein structural changes associated with S-nitrosylation of a myoglobin protein.Structure-guided design of fluorescent protein-based imaging probes:
In this collaborative project with the laboratory of Loren Looger at HHMI-Janelia Farm Research Campus, we are using a structure-guided protein design approach to create or improve fluorescent protein-based sensors. The figure at right shows the crystal structure of the GCaMP calcium indicator protein comprising a circularly-permuted fluorescent protein domain (EGFP) fused to the calcium-binding protein calmoulin and a calmodulin target peptide (M13). We were able to demonstrate the large-scale conformational changes that occur as a consequence of calcium binding and alter the chemical environment of the fluorescent protein chromophore. This information has helped to produce improved GCaMP sensors by mutagenesis.Selected Peer-Reviewed Publications (ResearcherID)
Prince, R. N.; Schreiter, E. R.; Zou, P.; Wiley, H. S.; Ting, A. Y.; Lee, R. T.; Lauffenburger, D. A. “The heparin-binding domain of HB-EGF mediates localization to sites of cell-cell contact and prevents HB-EGF proteolytic release” Journal of Cell Science, 2010, 123, 2308.
Tian, L.; Hires, S. A.; Mao, T.; Huber, D.; Chiappe, M. E.; Chalasani, S. H.; Petreanu, L.; Akerboom, J.; McKinney, S. A.; Schreiter, E. R.; Bargmann, C. I.; Jayaraman V.; Svoboda, K.; Looger, L. L. "Imaging neural activity in worms, flies and mice with improved GCaMP calcium indicators" Nature Methods (2009) 6, 857.
Patwari, P.; Chutkow, W. A.; Cummings, K.; Verstraeten, V. L.; Lammerding, J.; Schreiter, E. R.; Lee, R. T. "Thioredoxin-independent regulation of metabolism by the alpha-arrestin proteins" Journal of Biological
Chemistry (2009) 284, 24996.
Akerboom J., Vélez Rivera J.D., Rodríguez Guilbe M.M., Alfaro Malavé E.C., Hernandez H.H., Tian L., Hires S.A., Marvin J.S., Looger L.L., Schreiter E.R. "Crystal structures of the GCaMP calcium sensor reveal the mechanism of fluorescence signal change and aid rational design" Journal of Biological Chemistry (2009) 284, 6455.
Rodriguez Guilbe, M. M.; Alfaro Malave, E. C.; Akerboom, J.; Marvin, J. S.; Looger, L. L.; Schreiter, E. R."Crystallization and preliminary X-ray characterization of the genetically encoded fluorescent calcium indicator protein GCaMP2" Acta Crystallographica Section F: Structural Biology and Crystallization Communications (2008) F64, 629.
Alfaro, E.; Sosa, L.; Sanoguet, Z.; Pastrana-Ríos, B.; Schreiter, E. R. "Crystallization and preliminary X-ray characterization of full-length Chlamydomonas reinhardtii centrin" Acta Crystallographica Section F: Structural Biology and Crystallization Communications (2008) F64, 402.
Phillips, C. M.*; Schreiter, E. R.*; Guo, Y.; Wang, S. C.; Zamble, D. B.; Drennan, C. L. “Structural Basis of the Metal Specificity for Nickel Regulatory Protein NikR” Biochemistry (2008) 47, 1938.
*equal contributions
Schreiter, E. R. & Drennan C. L. “Ribbon-Helix-Helix Transcription Factors: Variations on a Theme” Nature Reviews Microbiology (2007) 5, 710.
Sanada, S.; Hakuno, D.; Higgins, L. J.; Schreiter, E. R.; McKenzie, A. N.; Lee, R. T. “IL-33 and ST2 comprise a critical biomechanically induced and cardioprotective signaling system” Journal of Clinical Investigation (2007) 117, 1538.
Schreiter, E. R.; Rodríguez, M.M.; Weichsel, A.; Montfort, W.R.; Bonaventura, J. “S-nitrosylation-induced conformational change in blackfin tuna myoglobin” Journal of Biological Chemistry (2007) 282, 19773.
Yoshioka, J.; Schreiter, E. R.; Lee, R. T. “Role of thioredoxin in cell growth through interactions with signaling molecules” Antioxidants & Redox Signaling (2006) 8, 2143.
Schreiter, E. R.; Wang, S. C.; Zamble, D. B.; Drennan, C. L. “NikR-operator complex structure and the mechanism of repressor activation by metal ions” Proceedings of the National Academy of Sciences, USA (2006) 103, 13676.
Schreiter, E. R.; Sintchak, M. D.; Guo, Y.; Chivers, P. T.; Sauer, R. T.; Drennan, C. L. “Crystal structure of the nickel-responsive transcription factor NikR” Nature Structural Biology (2003) 10, 794.
Drennan, C. D.; Heo, J.; Sintchak, M. D.; Schreiter, E.; Ludden, P. W. “Life on carbon monoxide: X-ray Structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase” Proceedings of the National Academy of Sciences, USA (2001) 98, 11973.