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- W2062548426 endingPage "5634" @default.
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- W2062548426 abstract "Many stress proteins and their cognates function as molecular chaperones or as components of proteolytic systems. Viral infection can stimulate synthesis of stress proteins and particular associations of viral and stress proteins have been documented. However, demonstrations of functions for stress proteins in viral life cycles are few. We have initiated an investigation of the roles of stress proteins in eukaryotic viral life cycles using as a model the Ty3 retrovirus-like element of Saccharomyces cerevisiae. During stress, Ty3 transposition is inhibited; Ty3 DNA is not synthesized and, although precursor proteins are detected, mature Ty3 proteins and virus-like particles (VLPs) do not accumulate. The same phenotype is observed in the constitutively stressed ssa1 ssa2 mutant, which lacks two cytoplasmic members of the hsp70 family of chaperones. Ty3 VLPs preformed under nonstress conditions are degraded more rapidly if cells are shifted from 30 degrees C to 37 degrees C. These results suggest that Ty3 VLPs are destroyed by cellular stress proteins. Elevated expression of the yeast UBP3 gene, which encodes a protease that removes ubiquitin from proteins, allows mature Ty3 proteins and VLPs to accumulate in the ssa1 ssa2 mutant, suggesting that, at least under stress conditions, ubiquitination plays a role in regulating Ty3 transposition." @default.
- W2062548426 created "2016-06-24" @default.
- W2062548426 creator A5029367275 @default.
- W2062548426 creator A5042443736 @default.
- W2062548426 date "1996-05-28" @default.
- W2062548426 modified "2023-09-27" @default.
- W2062548426 title "Cellular stress inhibits transposition of the yeast retrovirus-like element Ty3 by a ubiquitin-dependent block of virus-like particle formation." @default.
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- W2062548426 doi "https://doi.org/10.1073/pnas.93.11.5629" @default.
- W2062548426 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/39299" @default.
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