B.S., Eötvös Lóránd University, Hungary, 1986
Ph.D., University of Pittsburgh, 1992
Research Statement
The current focus of the lab is to understand the molecular details of mechanisms by which protein activity can be modulated. To function properly, cells must coordinate and choreograph a large number of simultaneous events and processes. These are carried out by proteins. We use X-ray crystallography as our main tool to study the fine details of how the activity and function of protein-protein and protein-DNA complexes are regulated. We employ this approach as it is one of the few experimental techniques that produces high-resolution "snapshots" to visualize subtle changes in protein structure that often accompany functional regulation. With these snapshots in hand, we use a variety of biochemical, biophysical and simulation approaches to bridge the structures and biological function. For example, we are investigating how the movement of mobile genetic elements such as transposons or viruses is controlled. One of our current areas of emphasis is the Rep protein of adeno-associated virus (AAV); this protein catalyzes the integration of the AAV genome into a specific locus in human chromosome 19, making it an extremely useful tool for gene therapy studies. In addition, we are studying how a ubiquitous group of chaperone proteins known as 14-3-3s are able to direct when and where in a cell to deliver proteins that regulate gene expression.For more information, see my group on the Structural Biology Section home page.
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Selected Publications
1. Wickner RB, Dyda F, Tycko R Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register {beta}-sheet structure. Proc Natl Acad Sci U S A, 2008. [Full Text/Abstract]
2. Guynet C, Hickman AB, Barabas O, Dyda F, Chandler M, Ton-Hoang B In Vitro Reconstitution of a Single-Stranded Transposition Mechanism of IS608. Mol Cell(29): 302-312, 2008. [Full Text/Abstract]
3. Barabas O, Ronning DR, Guynet C, Hickman AB, Ton-Hoang B, Chandler M, Dyda F Mechanism of IS200/IS605 Family DNA Transposases: Activation and Transposon-Directed Target Site Selection. Cell(132): 208-20, 2008. [Full Text/Abstract]
4. Obsilova V, Nedbalkova E, Silhan J, Boura E, Herman P, Vecer J, Sulc M, Teisinger J, Dyda F, Obsil T The 14-3-3 Protein Affects the Conformation of the Regulatory Domain of Human Tyrosine Hydroxylase. Biochemistry(47): 1768-1777, 2008. [Full Text/Abstract]
5. Bradley CM, Jones S, Huang Y, Suzuki Y, Kvaratskhelia M, Hickman AB, Craigie R, Dyda F Structural basis for dimerization of LAP2alpha, a component of the nuclear lamina. Structure(15): 643-53, 2007. [Full Text/Abstract]
6. Ronning DR, Guynet C, Ton-Hoang B, Perez ZN, Ghirlando R, Chandler M, Dyda F Active site sharing and subterminal hairpin recognition in a new class of DNA transposases. Mol Cell (20): 143-54, 2005. [Full Text/Abstract]
7. Hickman AB, Dyda F Binding and unwinding: SF3 viral helicases. Curr Opin Struct Biol (15): 77-85, 2005. [Full Text/Abstract]
8. Hickman AB, Perez ZN, Zhou L, Musingarimi P, Ghirlando R, Hinshaw JE, Craig NL, Dyda F Molecular architecture of a eukaryotic DNA transposase. Nat Struct Mol Biol (12): 715-21, 2005. [Full Text/Abstract]
9. Bradley CM, Ronning DR, Ghirlando R, Craigie R, Dyda F Structural basis for DNA bridging by barrier-to-autointegration factor. Nat Struct Mol Biol (12): 935-6, 2005. [Full Text/Abstract]
10. Ton-Hoang B, Guynet C, Ronning DR, Cointin-Marty B, Dyda F, Chandler M Transposition of ISHp608, member of an unusual family of bacterial insertion sequences. EMBO J (24): 3325-38, 2005. [Full Text/Abstract]
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