Tim Formosa
University of Utah
67 Papers
405 Citations
Tim Formosa is an academic researcher from University of Utah. The author has contributed to research in topics: Nucleosome & Histone. The author has an hindex of 39, co-authored 61 publications. Previous affiliations of Tim Formosa include University of California, San Francisco & Harvard University.
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Papers
DNA synthesis dependent on genetic recombination: Characterization of a reaction catalyzed by purified bacteriophage T4 proteins
Tim Formosa,Bruce Alberts +1 more
TL;DR: To simulate a reaction that occurs in T4-infected cells, an in vitro DNA synthesis system that requires seven highly purified proteins encoded by this bacteriophage is developed: the DNA polymerase "holoenzyme" (four proteins), gene 32 protein, dda DNA helicase, and uvsX protein - an enzyme that catalyzes homologueous DNA pairing and is functionally homologous to the recA protein.
266
The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein.
Jacqueline Wittmeyer,Tim Formosa +1 more
TL;DR: It is shown that at the nonpermissive temperature, cdc68-1 mutants arrest as unbudded cells with a 1C DNA content, consistent with a possible role for Cdc68 in the prereplicative stage of the cell cycle.
223
The Role of FACT in Making and Breaking Nucleosomes
TL;DR: This review summarizes recent results that have begun to reveal how FACT can promote what appear to be contradictory goals, using a simple set of binding activities to both enhance and diminish the stability of nucleosomes.
222
Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin structure.
Tim Formosa,Susan Ruone,Melissa D. Adams,Aileen E. Olsen,Peter Eriksson,Yaxin Yu,Alison R. Rhoades,Paul D. Kaufman,David J. Stillman +8 more
TL;DR: In this article, Spt16/Cdc68, Pob3, and Nhp6 collaborate in vitro and in vivo as the yeast factor SPN, which is homologous to human FACT.
yFACT Induces Global Accessibility of Nucleosomal DNA without H2A-H2B Displacement
TL;DR: It is proposed that yFACT promotes a reversible transition between two nucleosomal forms, and that this activity contributes to the establishment and maintenance of the chromatin barrier as well as to overcoming it.
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