Computational methods for yeast prion curing curves

被引:1
|
作者
Ridout, Martin S. [1 ]
机构
[1] Univ Kent, Inst Math Stat & Actuarial Sci, Canterbury CT2 7NF, Kent, England
基金
英国生物技术与生命科学研究理事会;
关键词
Age-dependent branching process; Fast Fourier transform; Laplace transform numerical transform inversion; Renewal process; Saccharomyces cerevisiae;
D O I
10.1016/j.mbs.2008.07.008
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
if the chemical guanidine hydrochloride is added to a dividing culture of yeast cells in which some of the protein Sup35p is in its prion form. the proportion of cells that carry replicating units of the prion, termed propagons, decreases gradually over time. Stochastic models to describe this process of 'curing' have been developed in earlier work. The present paper investigates the use of numerical methods of Laplace transform inversion to calculate curing curves and contrasts this with an alternative, more direct, approach that involves numerical integration. Transform inversion is found to provide a much more efficient computational approach that allows different models to be investigated with minimal programming effort. The method is used to investigate the robustness of the curing curve to changes in the assumed distribution of cell generation times. Matlab code is available for carrying out the calculations. (C) 2008 Elsevier Inc. All rights reserved.
引用
收藏
页码:152 / 157
页数:6
相关论文
共 50 条
  • [21] Proteolysis suppresses spontaneous prion generation in yeast
    Okamoto, Atsushi
    Hosoda, Nao
    Tanaka, Anri
    Newnam, Gary P.
    Chernoff, Yury O.
    Hoshino, Shin-ichi
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2017, 292 (49) : 20113 - 20124
  • [22] Peptide sequences converting polyglutamine into a prion in yeast
    Odani, Wataru
    Urata, Kazuhiro
    Okuda, Momoko
    Okuma, Shunsuke
    Koyama, Hiroko
    Pack, Chan-Gi
    Fujiwara, Kei
    Nojima, Tatsuya
    Kinjo, Masataka
    Kawai-Noma, Shigeko
    Taguchi, Hideki
    FEBS JOURNAL, 2015, 282 (03) : 477 - 490
  • [23] Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements
    Hines, Justin K.
    Higurashi, Takashi
    Srinivasan, Mathangi
    Craig, Elizabeth A.
    PRION, 2011, 5 (04) : 238 - 244
  • [24] Curing of Yeast [URE3] Prion by the Hsp40 Cochaperone Ydj1p Is Mediated by Hsp70
    Sharma, Deepak
    Stanley, Robert F.
    Masison, Daniel C.
    GENETICS, 2009, 181 (01) : 129 - 137
  • [25] An insight into the complex prion-prion interaction network in the budding yeast Saccharomyces cerevisiae
    Du, Zhiqiang
    Valtierra, Stephanie
    Li, Liming
    PRION, 2014, 8 (06) : 387 - 392
  • [26] Mammalian amyloidogenic proteins promote prion nucleation in yeast
    Chandrannowlishwaran, Pavithra
    Sun, Meng
    Casey, Kristin L.
    Romanyuk, Andrey V.
    Grizel, Anastasiya V.
    Sopova, Julia V.
    Rubel, Aleksandr A.
    Nussbaum-Krammer, Carmen
    Vorberg, Ina M.
    Chernoff, Yury O.
    JOURNAL OF BIOLOGICAL CHEMISTRY, 2018, 293 (09) : 3436 - 3450
  • [27] Heritable Remodeling of Yeast Multicellularity by an Environmentally Responsive Prion
    Holmes, Daniel L.
    Lancaster, Alex K.
    Lindquist, Susan
    Halfmann, Randal
    CELL, 2013, 153 (01) : 153 - 165
  • [28] Physical Properties of Polymorphic Yeast Prion Amyloid Fibers
    Castro, Carlos E.
    Dong, Jijun
    Boyce, Mary C.
    Lindquist, Susan
    Lang, Matthew J.
    BIOPHYSICAL JOURNAL, 2011, 101 (02) : 439 - 448
  • [29] Comparative assay of amyloid and prion contents in yeast cells
    Nevzglyadova O.V.
    Kuznetsova I.M.
    Artemov A.V.
    Mikhailova E.V.
    Turoverov K.K.
    Soidla T.R.
    Cell and Tissue Biology, 2008, 2 (1) : 71 - 80
  • [30] Chaperone functional specificity promotes yeast prion diversity
    Killian, Andrea N.
    Hines, Justin K.
    PLOS PATHOGENS, 2018, 14 (01)