TY - JOUR
T1 - Protein-only inheritance in yeast
T2 - Something to get [PSI+]-ched about
AU - Serio, Tricia R.
AU - Lindquist, Susan L.
N1 - Funding Information:
We thank the many researchers whose work has collectively revealed the richness of [ PSI + ] biology. We apologize for the limited citations allowed owing to space constraints. We also thank Julie Feder for invaluable help with the figures. This work was supported by the Cancer Research Fund of the Damon Runyon–Walter Winchell Foundation Fellowship DRG-1436 to T.R.S. and NIH GM025874 to S.L.L. and the Howard Hughes Medical Institute.
PY - 2000/3/1
Y1 - 2000/3/1
N2 - Recent work suggests that two unrelated phenotypes, [PSI+] and [URE3], in the yeast Saccharomyces cerevisiae are transmitted by non-covalent changes in the physical states of their protein determinants, Sup35p and Ure2p, rather than by changes in the genes that encode these proteins. The mechanism by which alternative protein states are self-propagating is the key to understanding how proteins function as elements of epigenetic inheritance. Here, we focus on recent molecular-genetic analysis of the inheritance of the [PSI+] factor of S. cerevisiae. Insights into this process might be extendable to a group of mammalian diseases (the amyloidoses), which are also believed to be a manifestation of self-perpetuating changes in protein conformation.
AB - Recent work suggests that two unrelated phenotypes, [PSI+] and [URE3], in the yeast Saccharomyces cerevisiae are transmitted by non-covalent changes in the physical states of their protein determinants, Sup35p and Ure2p, rather than by changes in the genes that encode these proteins. The mechanism by which alternative protein states are self-propagating is the key to understanding how proteins function as elements of epigenetic inheritance. Here, we focus on recent molecular-genetic analysis of the inheritance of the [PSI+] factor of S. cerevisiae. Insights into this process might be extendable to a group of mammalian diseases (the amyloidoses), which are also believed to be a manifestation of self-perpetuating changes in protein conformation.
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U2 - 10.1016/S0962-8924(99)01711-0
DO - 10.1016/S0962-8924(99)01711-0
M3 - Review article
C2 - 10675903
AN - SCOPUS:0034160086
SN - 0962-8924
VL - 10
SP - 98
EP - 105
JO - Trends in Cell Biology
JF - Trends in Cell Biology
IS - 3
ER -