个人简介

B.S., Utah State University Ph.D., Duke University Postdoctoral, Duke University Postdoctoral, University of Utah

研究领域

Biochemistry

X-ray crystallography, structure and mechanism of proteins The broad goal of our research is to understand biological function at a molecular level. Since biological activity is derived from the three-dimensional structure of a system, mechanistic details are often best described in the context of detailed structural information. The basic approach of the lab is to use x-ray crystallography techniques in combination with biochemical analysis to understand the structure and mechanism of proteins and macromolecular assemblies. The lab has a strong interest in protein-nucleic acid interactions. Our current work focuses on themes central to replication and transcription. A particular emphasis is placed on proteins and complexes associated with regulation and coordination of replication and transcription processes.

近期论文

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Bakelar, J., Sliwa, D. and Johnson, S.J.* (2013). “Crystal structures of S-HPCDH reveal determinants of stereospecificity for R- and S-hydroxypropyl-coenzyme M dehydrogenases.” Archives of Biochemistry and Biophysics 533 (1-2):62-68. Zeng, J., Lytle, A.K., Gage, D., Johnson, S.J. and Zhan, J.* (2013). “Specific chlorination of isoquinolines by a fungal flavin-dependent halogenase.” Bioorganic and Medicinal Chemistry Letters 23 (4):1001-1003. Johnson, S.J.* and Jackson, R.N. (2013). “Structures of Ski2-like RNA helicases: common themes and complex assemblies.” RNA Biology 10 (1):33-43. Kuznetsov, V.I., Hengge, A.C.* and Johnson, S.J.* (2012) “New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening.” Biochemistry 51(49):9869-79. Schaeffer, D., Reis, F.P., Johnson, S.J., Arraiano, C.M. and van Hoof, A.* (2012). “The CR3 motif of Rrp44p is important for interaction with the core exosome and exosome function.” Nucleic Acids Research. (in press). Brandão, T.A.S., Johnson, S.J.* and Hengge, A.C.* (2012).The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B. Archives of Biochemistry and Biophysics. 525(1):53-59. Gui, L., Wooderchack, W., Porter, P., Daly, M., Johnson, S.J. and Hevel, J.M.* (2011). Investigation of the Molecular Origins of Protein Arginine Methyltransferase I (PRMT1) Product Specificity Reveals a Role for Two Conserved Methionine Residues. Journal of Biological Chemistry. 286(33):29118-29126. Close, D., Johnson, S.J., Sadano, M., McDonald, S., Robinson, H. and Hill, C.P.* (2011). Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain. Journal of Molecular Biology. 408(4):697-713. Hintze, B.J. and Johnson, S.J. (2010). ResDe: A New Tool for Visual Definition of Distance Restraints for Crystallographic Refinement. The Journal of Applied Crystallography 43, 1540-1542. Jackson, R.N., Klauer, A.A., Hintze, B.J., Robinson, H., van Hoof, A. and S. J. Johnson, S.J. (2010). The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. The EMBO Journal. 29, 2205-2216. Brandão, T.A.S., Hengge, A.C. and Johnson, S.J. (2010) Insights into the reaction of protein tyrosine phosphatase 1B. Crystal structures for transition-state analogs of both catalytic steps. Journal of Biological Chemistry. 285(21):15874-83. Brandão, T.A.S., Robinson, H., Johnson, S.J., and Hengge, A.C. (2009) Impaired acid catalysis by mutation of a protein loop hinge residue in a YopH mutant revealed by crystal structures. Journal of the American Chemical Society. 131(2), 778–786. Johnson SJ, Close D, Robinson H, Vallet-Gely I, Dove SL, Hill CP. (2008) Crystal structure and RNA binding of the Tex protein from Pseudomonas aeruginosa. J Mol Biol, 377, 1460-73. Johnson, S.J., Beese, L.S. (2004) Structures of mismatch replication errors observed in a DNA polymerase. Cell 116, 803-816. Johnson, S.J., Taylor, J.S., Beese, L.S. (2003) Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proc Natl Acad Sci USA, 100, 3895-3900.