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You searched for subject:(Hsp82). Showing records 1 – 2 of 2 total matches.

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University of Alberta

1. Mai, BaoChan N. The Biochemical Characterization of the ATPase activity of three Hsp82 point mutants: Hsp82pA587T, Hsp82pG313S, and Hsp82pE381K.

Degree: MS, Department of Cell Biology, 2012, University of Alberta

Chaperones are family of proteins that assist in protein folding. 90 kDa Heat shock protein (Hsp90 mammalians, Hsp82 in Saccharomyces cerevisiae) is a well conserved chaperone that is essential for eukaryotic viability. The Hsp90 cycle is regulated by the ability to hydrolyze ATP, and through the interactions with other proteins known as co-chaperones. I biochemically characterized three Hsp82 point mutants: Hsp82pA587T, Hsp82pG313S, and Hsp82pE381K, using co-chaperones known to influence the ATPase activity of Hsp82p (Aha1p, Sti1p, Sba1p, and Hch1p). The ATPase activity of the Hsp82pG313S mutant could not characterize due to the low signal to noise ratio. I discovered the Hsp82pA587T mutant ATPase activity was over stimulated by Aha1p, but had a similar relationship as the wild-type in terms of the Sti1p and Sba1p. With the Hsp82pE381K mutant, I observed that the mutant was not stimulated robustly by Aha1p, and this stimulated rate was not inhibited by Sti1p.

Subjects/Keywords: Hsp82; ATPase; Biochemical

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APA (6th Edition):

Mai, B. N. (2012). The Biochemical Characterization of the ATPase activity of three Hsp82 point mutants: Hsp82pA587T, Hsp82pG313S, and Hsp82pE381K. (Masters Thesis). University of Alberta. Retrieved from https://era.library.ualberta.ca/files/c534fp07w

Chicago Manual of Style (16th Edition):

Mai, BaoChan N. “The Biochemical Characterization of the ATPase activity of three Hsp82 point mutants: Hsp82pA587T, Hsp82pG313S, and Hsp82pE381K.” 2012. Masters Thesis, University of Alberta. Accessed October 20, 2020. https://era.library.ualberta.ca/files/c534fp07w.

MLA Handbook (7th Edition):

Mai, BaoChan N. “The Biochemical Characterization of the ATPase activity of three Hsp82 point mutants: Hsp82pA587T, Hsp82pG313S, and Hsp82pE381K.” 2012. Web. 20 Oct 2020.

Vancouver:

Mai BN. The Biochemical Characterization of the ATPase activity of three Hsp82 point mutants: Hsp82pA587T, Hsp82pG313S, and Hsp82pE381K. [Internet] [Masters thesis]. University of Alberta; 2012. [cited 2020 Oct 20]. Available from: https://era.library.ualberta.ca/files/c534fp07w.

Council of Science Editors:

Mai BN. The Biochemical Characterization of the ATPase activity of three Hsp82 point mutants: Hsp82pA587T, Hsp82pG313S, and Hsp82pE381K. [Masters Thesis]. University of Alberta; 2012. Available from: https://era.library.ualberta.ca/files/c534fp07w

2. Zemska, Olga. Discovery Of Intracellular Growth Requirements of the Fungal Pathogen <i>Histoplasma capsulatum</i>.

Degree: MS, Microbiology, 2012, The Ohio State University

<i>Histoplasma capsulatum</i> is a pathogenic fungus endemic to the Ohio and Mississippi River valleys. Infection of mammals by <i>Histoplasma</i> causes respiratory histoplasmosis of varying severity which can lead to disseminated life-threatening disease. Upon inhalation into the mammalian lung, <i>Histoplasma</i> yeast are taken up by alveolar macrophages in which they replicate and ultimately lyse the host immune cells. <i>Histoplasma</i>’s virulence in these phagocytes and the inability of the immune system to control the infection highlights the need to understand the mechanisms underlying the pathogenicity of this fungus. We sought to identify <i>Histoplasma</i> genes required for survival and growth in macrophages. We optimized procedures for <i>Agrobacterium</i>-mediated transformation of <i>Histoplasma</i> to facilitate insertional mutagenesis, and developed a simple and efficient screen for <i>Histoplasma</i> mutants unable to lyse host macrophages. We identified 14 mutants from 6500 that had decreased virulence in phagocytes. One of the loci identified is a heat shock protein 90 homolog (<i>HSP82</i>) which we show is instrumental for <i>Histoplasma</i> yeast to adapt to infection-associated stresses. A second identified locus, a riboflavin biosynthesis enzyme (<i>RIB2</i>), indicates that <i>de novo</i> vitamin biosynthesis is required for fungal proliferation within host cells. Murine infections with these mutants confirm each is necessary for full <i>Histoplasma</i> virulence in mammalian hosts. The attenuation of the <i>rib2::T-DNA</i> mutant suggests that the mammalian phagosome is a vitamin-limiting environment. Using folate biosynthesis inhibitors to arrest intracellular <i>Histoplasma</i> growth, we show that <i>Histoplasma</i> also requires <i>de novo</i> synthesis of folate intermediates. Together, these data demonstrate that <i>de novo</i> vitamin biosynthesis enables <i>Histoplasma</i> yeast to replicate in the nutrient-limiting macrophage phagosome and highlights vitamin biosynthetic pathways as potential therapeutic targets for treatment of histoplasmosis. Advisors/Committee Members: Rappleye, Chad (Committee Chair).

Subjects/Keywords: Genetics; Microbiology; Molecular Biology; Parasitology; Histoplasma capsulatum; fungal pathogen; Agrobacterium tumefaciens-mediated transformation of fungi; insertional mutagenesis; intramacrophage replication; HSP82; de novo vitamin biosynthesis; riboflavin; folate; antifungal drug therapy

…27 Chapter 3: Discovery of a role for Hsp82 in Histoplasma virulence through a quantitative… …50 3.3.3 Involvement of Hsp82 in Histoplasma stress tolerance… …54 Figure 8. Mutant 16E1 contains a T-DNA insertion that decreases HSP82 expression .. 55… …Figure 9. Complementation of HSP82 restores yeast virulence in P388D1-lacZ macrophages… …56 Figure 10. HSP82 is required for full Histoplasma virulence in vivo… 

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Zemska, O. (2012). Discovery Of Intracellular Growth Requirements of the Fungal Pathogen <i>Histoplasma capsulatum</i>. (Masters Thesis). The Ohio State University. Retrieved from http://rave.ohiolink.edu/etdc/view?acc_num=osu1343803044

Chicago Manual of Style (16th Edition):

Zemska, Olga. “Discovery Of Intracellular Growth Requirements of the Fungal Pathogen <i>Histoplasma capsulatum</i>.” 2012. Masters Thesis, The Ohio State University. Accessed October 20, 2020. http://rave.ohiolink.edu/etdc/view?acc_num=osu1343803044.

MLA Handbook (7th Edition):

Zemska, Olga. “Discovery Of Intracellular Growth Requirements of the Fungal Pathogen <i>Histoplasma capsulatum</i>.” 2012. Web. 20 Oct 2020.

Vancouver:

Zemska O. Discovery Of Intracellular Growth Requirements of the Fungal Pathogen <i>Histoplasma capsulatum</i>. [Internet] [Masters thesis]. The Ohio State University; 2012. [cited 2020 Oct 20]. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1343803044.

Council of Science Editors:

Zemska O. Discovery Of Intracellular Growth Requirements of the Fungal Pathogen <i>Histoplasma capsulatum</i>. [Masters Thesis]. The Ohio State University; 2012. Available from: http://rave.ohiolink.edu/etdc/view?acc_num=osu1343803044

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