NR AJBV
AU Osherovich,L.Z.; Weissman,J.S.
TI Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion
QU Cell 2001 Jul 27; 106(2): 183-94
PT journal article
AB The yeast prion [PSI(+)] results from self-propagating aggregates of Sup35p. De novo formation of [PSI(+)] requires an additional non-Mendelian trait, thought to result from a prion form of one or more unknown proteins. We find that the Gln/Asn-rich prion domains of two proteins, New1p and Rnq1p, can control susceptibility to [PSI(+)] induction as well as enhance aggregation of a human glutamine expansion disease protein. [PSI(+)] inducibility results from gain-of-function properties of New1p and Rnq1p aggregates rather than from inactivation of the normal proteins. These studies suggest a molecular basis for the epigenetic control of [PSI(+)] inducibility and may reveal a broader role for this phenomenon in the physiology of protein aggregation.
MH Amino Acid Sequence; Asparagine/chemistry/genetics/*metabolism; Fungal Proteins/*chemistry/genetics/*metabolism; Gene Expression; Genes, Fungal/genetics; Glutamine/chemistry/genetics/*metabolism; Human; Machado-Joseph Disease/metabolism; Microscopy, Fluorescence; Molecular Chaperones/chemistry/genetics/metabolism; Molecular Sequence Data; Nerve Tissue Proteins/chemistry/metabolism; Peptides/chemistry/genetics/metabolism; Phenotype; Prions/*chemistry/genetics/*metabolism; Protein Binding; Protein Structure, Tertiary; Recombinant Fusion Proteins/chemistry/metabolism; Saccharomyces cerevisiae/chemistry/cytology/genetics/*metabolism; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.
AD Howard Hughes Medical Institute, Department of Cellular and Molecular Pharmacology, University of California-San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143, USA. lxoshe@itsa.ucsf.edu
SP englisch
PO USA