The primary structure of the mammalian prion protein is completely different from that of
the yeast prion protein.
The helpful
yeast prion protein and the dangerous mammalian prion protein have virtually nothing in common.
Yeast can also carry prions, and the duo fused part of
a yeast prion protein called Sup35 to a normal rat protein that controls the transcription of DNA into RNA.
Not exact matches
Study coauthor Susan Lindquist of the Whitehead Institute for Biomedical Research in Cambridge, Mass., and her colleagues devised a way to test plant
proteins for
prion power by swapping bits of them into
yeast prions.
(stock image) Whitehead Institute scientists inserted the Arabidopsis thaliana
protein Luminidependens (LD) into
yeast to determine whether it has the traits of a
prion.
To see if the candidates have the properties of
prions, the scientists inserted the
proteins into
yeast, a model that the Lindquist lab has studied extensively.
Moreover, when the
protein snippet was inserted into
yeast, it could replace the functions of a known
prion - forming
yeast protein.
After consulting with Susan Lindquist, a
yeast -
prion expert at the Whitehead Institute for Biomedical Research in Cambridge, Massachusetts, Kandel and Si fused the slug
protein with the
yeast -
prion protein and found that the
yeast - friendly CPEB acted like a
prion, shifting shape and causing the
proteins all around it to act identically in a very durable way.
Then Si noticed a molecular similarity in CPEB to a harmless
prion protein found in
yeast.
Not only that, but in the current issue of Molecular Cell, the Lindquist lab has identified a new
yeast prion and shown that a segment of this
protein also confers prionlike activity.
Meanwhile, Eisenberg and his group zoomed in on a
yeast prion, discovering that it had interlocking teeth like a zipper, which contorted the
proteins into a ropelike shape.
Previously, True and Whitehead Institute Director Susan Lindquist reported that a particular
yeast protein called Sup35 somehow altered the metabolic properties — or phenotype — of the cell when it «misfolded» into a
prion state.
Spontaneous Variants of the [RNQ +]
Prion in
Yeast Demonstrate the Extensive Conformational Diversity Possible with
Prion Proteins.
Remarkably, the same
yeast chaperone reacts with
prion proteins from mammals.
Neither Hsp 104 or GroEL interacted with any of the dozens of other
proteins tested, but each produced an effect on both
yeast and mammalian
prion proteins.
Although the
yeast cells in these micrographs are expressing specific
prion - like
proteins (green, expressed
protein label along top of micrographs), neither
yeast containing
prion - like
proteins or the control exhibit the large
protein masses expected in cells expressing
prions.
Sondheimer focused his search on a handful of suspect
proteins that possessed regions that looked a lot like the
prion - determining regions of known
yeast prions Sup35 and Ure2.
December 9, 1997 Discovery links new form of inheritance in
yeast to «mad - cow» type diseases Researchers from the Howard Hughes Institute at the University of Chicago have discovered that a chaperone
protein from
yeast, which helps
proteins to change their shapes, controls a new,
protein - only form of inheritance, called a
yeast prion.
Whitehead Institute scientists performed an unbiased screen in
yeast cells that identifed dozens of
prion - like
proteins.
Researchers from the Howard Hughes Institute at the University of Chicago have discovered that a chaperone
protein from
yeast, which helps
proteins to change their shapes, controls a new,
protein - only form of inheritance, called a
yeast prion.
Although the
yeast sup35
protein and the mammalian
prion protein are not at all related to each other — the
yeast pose no risk to consumers of bread or beer — the researchers think that in - depth analysis of the
yeast prion - like elements and other
proteins that help them fold up may lead to new approaches to therapies for neurodegenerative diseases.
«The
yeast and the mammalian
prion proteins are genetically, structurally and functionally entirely different,» said Lindquist.
«We already know that two of the 6,200
proteins in
yeast can be
prions,» said Sondheimer.