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Permanent link (DOI): https://doi.org/10.7939/R3G31M

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The Biochemical Characterization of the ATPase activity of three Hsp82 point mutants: Hsp82pA587T, Hsp82pG313S, and Hsp82pE381K Open Access

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Other title
Subject/Keyword
Hsp82
ATPase
Biochemical
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Mai, BaoChan N
Supervisor and department
Paul LaPointe
Examining committee member and department
Andrew MacMillan (Biochemistry)
Gary Eitzen (Cell Biology)
Ben Montpetit (Cell Biology)
Department
Department of Cell Biology
Specialization

Date accepted
2012-09-28T13:05:14Z
Graduation date
2012-09
Degree
Master of Science
Degree level
Master's
Abstract
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.
Language
English
DOI
doi:10.7939/R3G31M
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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