Timothy G. Formosa, Ph.D.

Research Interests

  • Chromatin
  • Histone Chaperones
  • Chromatin Assembly and Disassembly
  • DNA Packaging
  • Cell Division

Languages

  • English

Academic Information

  • Departments: Biochemistry - Professor
  • Cancer Center Programs: Nuclear Control of Cell Growth & Differentiation

Academic Office Information

  • (801) 581-5435
  • Emma Eccles Jones Research Building
    Biochemistry
    15 North Medical Drive East, Room: 5520N
    Salt Lake City, UT 84112

Academic Bio

Tim Formosa, PhD, is a professor in the Department of Biochemistry at the University of Utah and a member of the Nuclear Control of Cell Growth and Differentiation Program at Huntsman Cancer Institute.Formosa studies how genetic material (DNA) is packaged and copied so that daughter cells each receive an accurate copy of the genetic instructions. Mistakes in this process are responsible for human cancers, but the machinery is common to many species. Formosa therefore uses single-celled yeasts to study the universal parts of the copying machinery because this allows the use of many experimental approaches that cannot be applied to larger animals, revealing the important principles that can then be tested in humans.Topics of study include--How histone chaperones participate in organizing and disassembling DNA packaging--How DNA is copied and assembled into chromatin, the stable form of DNA found in cells--How the packaging of DNA affects its accurate replication during cell divisionFormosa received a bachelor's degree from the University of California, Davis, and a PhD from the University of California, San Francisco.

Education History

Type School Degree
Postdoctoral Fellowship University of Washington
Genetics
Postdoctoral Fellow
Doctoral Training University of California at San Francisco
Biochemistry & Biophysics
Ph.D.
Undergraduate University of California at Davis
Biochemistry
B.S.

Selected Publications

Journal Article

  1. The FACT histone chaperone guides histone H4 into its nucleosomal conformation in Saccharomyces cerevisiae.McCullough L, Poe B, Connell Z, Xin H, Formosa T (2013). The FACT histone chaperone guides histone H4 into its nucleosomal conformation in Saccharomyces cerevisiae. Genetics, 195(1), 101-13.
  2. Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT.Kemble DJ, Whitby FG, Robinson H, McCullough LL, Formosa T, Hill CP (2013). Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT. J Biol Chem, 288(15), 10188-94.
  3. Structure of a proteasome Pba1-Pba2 complex: implications for proteasome assembly, activation, and biological function.Stadtmueller BM, Kish-Trier E, Ferrell K, Petersen CN, Robinson H, Myszka DG, Eckert DM, Formosa T, Hill CP (2012). Structure of a proteasome Pba1-Pba2 complex: implications for proteasome assembly, activation, and biological function. J Biol Chem, 287(44), 37371-82.
  4. Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain.Close D, Johnson SJ, Sdano MA, McDonald SM, Robinson H, Formosa T, Hill CP (2011). Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain. J Mol Biol, 408(4), 697-713.
  5. Insight into the mechanism of nucleosome reorganization from histone mutants that suppress defects in the FACT histone chaperone.McCullough L, Rawlins R, Olsen A, Xin H, Stillman DJ, Formosa T (2011). Insight into the mechanism of nucleosome reorganization from histone mutants that suppress defects in the FACT histone chaperone. Genetics, 188(4), 835-46.

Review

  1. The role of FACT in making and breaking nucleosomes.Formosa T (2012). The role of FACT in making and breaking nucleosomes. [Review]. Biochim Biophys Acta, 1819(3-4), 247-55.
  2. A kinase's work is never done: Rad53 monitors chromatin near replication origins.Formosa T (2011). A kinase's work is never done: Rad53 monitors chromatin near replication origins. [Review]. Cell Cycle, 10(4), 573-4.