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.
University of Washington
University of California at San Francisco
University of California at Davis
- Connell Z, Parnell TJ, McCullough LL, Hill CP, Formosa T (2021). The interaction between the Spt6-tSH2 domain and Rpb1 affects multiple functions of RNA Polymerase II. Nucleic Acids Res, 50(2), 784-802.
- Sivkina AL, Karlova MG, Valieva ME, McCullough LL, Formosa T, Shaytan AK, Feofanov AV, Kirpichnikov MP, Sokolova OS, Studitsky VM (2022). Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT. Commun Biol, 5(1), 2.
- Formosa T, Winston F (2020). The role of FACT in managing chromatin: disruption, assembly, or repair? Nucleic Acids Res, 48(21), 11929-11941.
- Chun Y, Joo YJ, Suh H, Batot G, Hill CP, Formosa T, Buratowski S (2019). Selective Kinase Inhibition Shows That Bur1 (Cdk9) Phosphorylates the Rpb1 Linker In Vivo. Mol Cell Biol, 39(15).
- McCullough LL, Pham TH, Parnell TJ, Connell Z, Chandrasekharan MB, Stillman DJ, Formosa T (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.
- Nune M, Morgan MT, Connell Z, McCullough L, Jbara M, Sun H, Brik A, Formosa T, Wolberger C (2019). FACT and Ubp10 collaborate to modulate H2B deubiquitination and nucleosome dynamics. Elife, 8.
- Chang HW, Nizovtseva EV, Razin SV, Formosa T, Gurova KV, Studitsky VM (2019). Histone Chaperone FACT and Curaxins: Effects on Genome Structure and Function. J Cancer Metastasis Treat, 5.
- 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.
- 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.
- 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.
- Formosa T (2012). The role of FACT in making and breaking nucleosomes. Biochim Biophys Acta, 1819(3-4), 247-55.
- 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.
- 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.
- Formosa T, Barry J, Alberts BM, Greenblatt J (1991). Using protein affinity chromatography to probe structure of protein machines. Methods Enzymol, 208, 24-45.
- Formosa T, Alberts BM (1986). DNA synthesis dependent on genetic recombination: characterization of a reaction catalyzed by purified bacteriophage T4 proteins. Cell, 47(5), 793-806.
- Formosa T, Alberts BM (1986). Purification and characterization of the T4 bacteriophage uvsX protein. J Biol Chem, 261(13), 6107-18.
- Griffith J, Formosa T (1985). The uvsX protein of bacteriophage T4 arranges single-stranded and double-stranded DNA into similar helical nucleoprotein filaments. J Biol Chem, 260(7), 4484-91.
- Jongeneel CV, Formosa T, Alberts BM (1984). Purification and characterization of the bacteriophage T4 dda protein. A DNA helicase that associates with the viral helix-destabilizing protein. J Biol Chem, 259(20), 12925-32.
- Jongeneel CV, Formosa T, Munn M, Alberts BM (1984). Enzymological studies of the T4 replication proteins. Adv Exp Med Biol, 179, 17-33.
- Formosa T, Alberts BM (1984). The use of affinity chromatography to study proteins involved in bacteriophage T4 genetic recombination. Cold Spring Harb Symp Quant Biol, 49, 363-70.
- Formosa T, Burke RL, Alberts BM (1983). Affinity purification of bacteriophage T4 proteins essential for DNA replication and genetic recombination. Proc Natl Acad Sci U S A, 80(9), 2442-6.
- Alberts BM, Barry J, Bedinger P, Formosa T, Jongeneel CV, Kreuzer KN (1983). Studies on DNA replication in the bacteriophage T4 in vitro system. Cold Spring Harb Symp Quant Biol, 47 Pt 2, 655-68.
- Formosa T (2011). A kinase's work is never done: Rad53 monitors chromatin near replication origins. Cell Cycle (10(4), pp. 573-4). United States.