A Systematic Survey Identifies Prions and Illuminates Sequence Features of Prionogenic Proteins
Name
Lindquist2.pdf
Description
main article
Size
2.22 MB
Format
Adobe PDF
Checksum (MD5)
d72b24c42880fd213fb0a8a43bfd6a15
Author(s)
Kapila, Atul
Halfmann, Randal Arthur
Lindquist, Susan
King, Oliver D.
Alberti, Simon
Date Issued
April 2009
Journal
Cell
Publisher
Elsevier
Citation
Alberti, Simon et al. “A Systematic Survey Identifies Prions and Illuminates Sequence Features of Prionogenic Proteins.” Cell137.1 (2009): 146-158.
Version
Author's final manuscript
Abstract
Prions are proteins that convert between structurally and functionally distinct states, one or more of which is transmissible. In yeast, this ability allows them to act as non-Mendelian elements of phenotypic inheritance. To further our understanding of prion biology, we conducted a bioinformatic proteome-wide survey for prionogenic proteins in S. cerevisiae, followed by experimental investigations of 100 prion candidates. We found an unexpected amino acid bias in aggregation-prone candidates and discovered that 19 of these could also form prions. At least one of these prion proteins, Mot3, produces a bona fide prion in its natural context that increases population-level phenotypic heterogeneity. The self-perpetuating states of these proteins present a vast source of heritable phenotypic variation that increases the adaptability of yeast populations to diverse environments.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
Persistent DSpace Link
DOI of Published Version
http://dx.doi.org/10.1016/j.cell.2009.02.044
