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.

Tools

Selected Publications

Johnson, S.J. and Jackson, R.N. (2012). Structures of Ski2-like RNA helicases: common themes and complex assemblies. RNA Biology (in press).

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 40 (18): 9298-9307.

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. 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. Journal of Molecular Biology. 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.