Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride
Byrne, L., Cox, B., Coleman, D., Ridout, M., Morgan, B. and Tuiteq, M. 2007. Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride. Proceedings of the National Academy of Sciences of the United States of America (PNAS). 104 (28), pp. 11688-11693.
|Authors||Byrne, L., Cox, B., Coleman, D., Ridout, M., Morgan, B. and Tuiteq, M.|
Guanidine hydrochloride (Gdn·HCl) blocks the propagation of yeast prions by inhibiting Hsp104, a molecular chaperone that is absolutely required for yeast prion propagation. We had previously proposed that ongoing cell division is required for Gdn·HCl-induced loss of the [PSI+] prion. Subsequently, Wu et al.[Wu Y, Greene LE, Masison DC, Eisenberg E (2005) Proc Natl Acad Sci USA 102:12789–12794] claimed to show that Gdn·HCl can eliminate the [PSI+] prion from α-factor-arrested cells leading them to propose that in Gdn·HCl-treated cells the prion aggregates are degraded by an Hsp104-independent mechanism. Here we demonstrate that the results of Wu et al. can be explained by an unusually high rate of α-factor-induced cell death in the [PSI+] strain (780-1D) used in their studies. What appeared to be no growth in their experiments was actually no increase in total cell number in a dividing culture through a counterbalancing level of cell death. Using media-exchange experiments, we provide further support for our original proposal that elimination of the [PSI+] prion by Gdn·HCl requires ongoing cell division and that prions are not destroyed during or after the evident curing phase.
|Journal||Proceedings of the National Academy of Sciences of the United States of America (PNAS)|
|Journal citation||104 (28), pp. 11688-11693|
|Publisher||National Academy of Sciences|
|Digital Object Identifier (DOI)||doi:10.1073/pnas.0701392104|
|10 Jul 2007|
|Publication process dates|
|Deposited||14 May 2015|
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