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

• Author / Creator

  Mai, BaoChan N

• 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

  • ATPase
  • Hsp82
  • Biochemical

• Graduation date

  Fall 2012

• Type of Item

  Thesis

• Degree

  Master of Science

• DOI

  https://doi.org/10.7939/R3G31M

• License

  This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.