Your English writing platform
Discover LudwigExact(9)
In its prion state, Rnq1, however, is aggregated and promotes the polymerization of Sup35 as well as of other polyQ-containing proteins [22], [28].
If NMPM-CSC were in its prion form, most of the protein would be expected to be aggregated.
DOI: http://dx.doi.org/10.7554/eLife.02949.005 10.7554/eLiFigure49.006 Figure 3. Converted Sup35 NM can remain in its prion conformation in E. coli cells lacking New1.
Having previously shown that Sup35 NM can adopt an infectious amyloid conformation in the E. coli cytoplasm (Garrity et al., 2010), we wished to determine whether or not E. coli cells could stably propagate Sup35 NM in its prion form.
We show that the age-associated deposit collects endogenous protein aggregates formed by Sup35 in its prion [ PSI+] form, and that this Sup35-enriched deposit is asymmetrically retained by the mother cells during cell division.
NMPM-CSC as the sole copy of Sup35p can be induced and propagated in its prion state, [ CHI+PM] (for chimeric [ PSI+], PM for P. methanolica), in S. cerevisiae [ 36, 37].
Similar(51)
Aggregation of FUS and TDP-43 has been shown to rely on regions resembling prion domains [ 94, 102, 179] and mutations in TDP-43 associated with ALS occur mainly in its prion-like region (Fig. 1).
Adriano Aguzzi, a neuropathologist at the University of Zurich in Switzerland, and his colleagues, wanted to trace the way normal protein converts into its prion form in mice.
We conclude that cells lacking ClpB cannot propagate Sup35 NM in its infectious prion conformation.
We previously demonstrated that conversion of Sup35 NM to its prion form in Escherichia coli, as in S. cerevisiae, depends on [ PIN+], which is formed by providing the bacterial cells with the yeast New1 protein (Garrity et al., 2010).
(A ) Cartoon representation of how Sup35 NM can convert to its prion form in the presence of New1 and remain in the prion conformation after cells have been cured of New1-encoding DNA.
More suggestions(2)
Write better and faster with AI suggestions while staying true to your unique style.
Since I tried Ludwig back in 2017, I have been constantly using it in both editing and translation. Ever since, I suggest it to my translators at ProSciEditing.

Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com