Premium
[ PIN + ]ning down [ PSI + ] inducibility
Author(s) -
Brechtel Teal M,
Villali Janice,
Davis Jason,
Pei Fen,
Sindi Suzanne S,
Serio Tricia R
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.lb42
Subject(s) - yeast , chaperone (clinical) , phenotype , structural biology , chemistry , computational biology , microbiology and biotechnology , biophysics , biology , biochemistry , gene , medicine , pathology
Prion proteins confer new phenotypes on cells by adopting an alternative conformation that changes their function and by templating the conversion of normally folded protein to the same state. While we understand how prion proteins in yeast maintain themselves in cells and colonies once they arise, the mechanism by which the alternative conformations of prion proteins first appear is poorly understood. To address this open question, our studies focus on the [ PSI + ] prion, an alternative conformation of the Sup35 protein. [ PSI + ] can only appear in yeast cells that also contain the [ PIN + ] prion, an alternative conformation of the Rnq1 protein. Our genetic studies suggest that [ PSI + ] appearance is sensitive to the level of the molecular chaperone Hsp104. Moreover, existing [ PSI + ] is sensitive to changes in Hsp104 levels in a [ PIN + ]‐ dependent manner. Together, our observations are consistent with a model in which [ PIN + ] acts as a decoy for chaperones and thereby promotes the persistence of nascent [ PSI + ]. Support or Funding Information This work was supported by NIH Training Grant T32 GM008659 to TMB and NIH Research Project Grants R01 GM100740 and R35 GM118042 to TRS. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .