Timothy G. Formosa

Timothy G. Formosa, PhD

Languages spoken: English

Academic Information

Departments Primary - Biochemistry

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 and packaging 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 gene expression and accurate replication of chromosomes during cell division

Formosa received a bachelor's degree from the University of California, Davis, and a PhD from the University of California, San Francisco.

Education History

Undergraduate University of California at Davis
 BS
Doctoral Training University of California at San Francisco
 PhD
Postdoctoral Fellowship University of Washington
 Postdoctoral Fellow

Selected Publications

Journal Article

  1. Jongeneel CV, Formosa T, Munn M, Alberts BM (1984). Enzymological studies of the T4 replication proteins. Adv Exp Med Biol, 179, 17-33.
  2. Formosa (2012). The role of FACT in making and breaking nucleosomes. Biochimica et biophysica acta, 1819(3-4), 247-55.
  3. Formosa T, Alberts B (1986). DNA synthesis dependent on genetic recombination: characterization of a reaction catalyzed by purified bacteriophage T4 proteins. Cell, 47(5), 793-806.
  4. Formosa T, Alberts B (1984). The use of affinity chromatography to study proteins involved in bacteriophage T4 genetic recombination. Cold Spring Harbor symposia on quantitative biology, 49, 363-70.
  5. Alberts BM, Barry J, Bedinger P, Formosa T, Jongeneel CV, Kreuzer K (1983). Studies on DNA replication in the bacteriophage T4 in vitro system. Cold Spring Harbor symposia on quantitative biology, 47 Pt 2, 655-68.
  6. McCullough L, Rawlins R, Olsen A, Xin H, Stillman DJ, Formosa (2011). Insight into the mechanism of nucleosome reorganization from histone mutants that suppress defects in the FACT histone chaperone. Genetics, 188(4), 835-46.
  7. McCullough L, Poe B, Connell Z, Xin H, Formosa (2013). The FACT histone chaperone guides histone H4 into its nucleosomal conformation in Saccharomyces cerevisiae. Genetics, 195(1), 101-13.
  8. McCullough LL, Pham TH, Parnell TJ, Connell Z, Chandrasekharan MB, Stillman DJ, Formosa (2019). Establishment and Maintenance of Chromatin Architecture Are Promoted Independently of Transcription by the Histone Chaperone FACT and H3-K56 Acetylation in Saccharomyces cerevisiae. Genetics, 211(3), 877-892.
  9. Stadtmueller BM, Kish-Trier E, Ferrell K, Petersen CN, Robinson H, Myszka DG, Eckert DM, Formosa T, Hill C (2012). Structure of a proteasome Pba1-Pba2 complex: implications for proteasome assembly, activation, and biological function. The Journal of biological chemistry, 287(44), 37371-82.
  10. Kemble DJ, Whitby FG, Robinson H, McCullough LL, Formosa T, Hill C (2013). Structure of the Spt16 middle domain reveals functional features of the histone chaperone FACT. The Journal of biological chemistry, 288(15), 10188-94.
  11. Formosa T, Alberts B (1986). Purification and characterization of the T4 bacteriophage uvsX protein. The Journal of biological chemistry, 261(13), 6107-18.
  12. Griffith J, Formosa (1985). The uvsX protein of bacteriophage T4 arranges single-stranded and double-stranded DNA into similar helical nucleoprotein filaments. The Journal of biological chemistry, 260(7), 4484-91.
  13. Jongeneel CV, Formosa T, Alberts B (1984). Purification and characterization of the bacteriophage T4 dda protein. A DNA helicase that associates with the viral helix-destabilizing protein. The Journal of biological chemistry, 259(20), 12925-32.
  14. Close D, Johnson SJ, Sdano MA, McDonald SM, Robinson H, Formosa T, Hill C (2011). Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain. Journal of molecular biology, 408(4), 697-713.
  15. Formosa T, Barry J, Alberts BM, Greenblatt (1991). Using protein affinity chromatography to probe structure of protein machines. Methods in enzymology, 208, 24-45.
  16. Chun Y, Joo YJ, Suh H, Batot G, Hill CP, Formosa T, Buratowski (2019). Selective Kinase Inhibition Shows That Bur1 (Cdk9) Phosphorylates the Rpb1 Linker In Vivo. Molecular and cellular biology, 39(15),
  17. Formosa T, Winston (2020). The role of FACT in managing chromatin: disruption, assembly, or repair?. Nucleic acids research, 48(21), 11929-11941.
  18. Formosa T, Burke RL, Alberts B (1983). Affinity purification of bacteriophage T4 proteins essential for DNA replication and genetic recombination. Proceedings of the National Academy of Sciences of the United States of America, 80(9), 2442-6.
  19. Nune M, Morgan MT, Connell Z, McCullough L, Jbara M, Sun H, Brik A, Formosa T, Wolberger (2019). FACT and Ubp10 collaborate to modulate H2B deubiquitination and nucleosome dynamics. eLife, 8,
  20. Chang HW, Nizovtseva EV, Razin SV, Formosa T, Gurova KV, Studitsky V (2019). Histone Chaperone FACT and Curaxins: Effects on Genome Structure and Function. Journal of cancer metastasis and treatment, 5,
  21. Connell Z, Parnell TJ, McCullough LL, Hill CP, Formosa (2022). The interaction between the Spt6-tSH2 domain and Rpb1 affects multiple functions of RNA Polymerase II. Nucleic acids research, 50(2), 784-802.
  22. Sivkina AL, Karlova MG, Valieva ME, McCullough LL, Formosa T, Shaytan AK, Feofanov AV, Kirpichnikov MP, Sokolova OS, Studitsky V (2022). Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT. Communications biology, 5(1), 2.

Other

  1. Formosa (2011). A kinase's work is never done: Rad53 monitors chromatin near replication origins. Cell cycle (Georgetown, Tex.), 10(4), 573-4.