Abstract
The yeast nonchromosomal gene [URE3] is due to a prion form of the nitrogen regulatory protein Ure2p. It is a negative regulator of nitrogen catabolism and acts by inhibiting the transcription factor Gln3p. Ure2p residues 1–80 are necessary for prion generation and propagation. The C-terminal fragment retains nitrogen regulatory activity, albeit somewhat less efficiently than the full-length protein, and it also lowers the frequency of prion generation. The crystal structure of this C-terminal fragment, Ure2p(97–354), at 2.3 Å resolution is described here. It adopts the same fold as the glutathione S -transferase superfamily, consistent with their sequence similarity. However, Ure2p(97–354) lacks a properly positioned catalytic residue that is required for S -transferase activity. Residues within this regulatory fragment that have been indicated by mutational studies to influence prion generation have been mapped onto the three-dimensional structure, and possible implications for prion activity are discussed.
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Dates
Type | When |
---|---|
Created | 13 years, 1 month ago (July 26, 2012, 7:12 p.m.) |
Deposited | 3 years, 2 months ago (June 7, 2022, 1:38 a.m.) |
Indexed | 1 year, 2 months ago (July 1, 2024, 4:35 p.m.) |
Issued | 24 years, 6 months ago (Feb. 6, 2001) |
Published | 24 years, 6 months ago (Feb. 6, 2001) |
Published Online | 24 years, 6 months ago (Feb. 6, 2001) |
Published Print | 24 years, 6 months ago (Feb. 13, 2001) |
@article{Umland_2001, title={The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p}, volume={98}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.98.4.1459}, DOI={10.1073/pnas.98.4.1459}, number={4}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Umland, Timothy C. and Taylor, Kimberly L. and Rhee, Sangkee and Wickner, Reed B. and Davies, David R.}, year={2001}, month=feb, pages={1459–1464} }