Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 280, Issue 29, Pages 26873-26879Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M503973200
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- NIAID NIH HHS [AI058979] Funding Source: Medline
- NINDS NIH HHS [NS046478] Funding Source: Medline
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Little is currently known about the biochemical mechanism by which induced prion protein (PrP) conformational change occurs during mammalian prion propagation. In this study, we describe the reconstitution of PrPres amplification in vitro using partially purified and synthetic components. Overnight incubation of purified PrP27 - 30 and PrPC molecules at a molar ratio of 1: 250 yielded similar to 2-fold baseline PrPres amplification. Addition of various polyanionic molecules increased the level of PrPres amplification to similar to 10-fold overall. Polyanionic compounds that stimulated purified PrPres amplification to varying degrees included synthetic, homopolymeric nucleic acids such as poly( A) and poly(dT), as well as non-nucleic acid polyanions, such as heparan sulfate proteoglycan. Size fractionation experiments showed that synthetic poly( A) polymers must be > 0.2 kb in length to stimulate purified PrPres amplification. Thus, one possible set of minimal components for efficient conversion of PrP molecules in vitro may be surprisingly simple, consisting of PrP27 - 30, PrPC, and a stimulatory polyanionic compound.
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