Timothy G. Formosa
Professor
Department of Biochemistry
Huntsman Cancer Institute
United States of America
Biography
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.
Research Interest
DNA Packaging Histone Chaperones Chromatin Chromatin Assembly and Disassembly Cell Division
Publications
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Formosa T (2012). The role of FACT in making and breaking nucleosomes. [Review]. Biochim Biophys Acta, 1819(3-4), 247-55.
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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.
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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.
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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.
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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.
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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.
