Unknown

Dataset Information

0

Characterization of the interaction domains of Ure2p, a prion-like protein of yeast.


ABSTRACT: In the yeast Saccharomyces cerevisiae, the non-Mendelian inherited genetic element [URE3] behaves as a prion. A hypothesis has been put forward which states that [URE3] arises spontaneously from its cellular isoform Ure2p (the product of the URE2 gene), and propagates through interactions of the N-terminal domain of the protein, thus leading to its aggregation and loss of function. In the present study, various N- and C-terminal deletion mutants of Ure2p were constructed and their cross-interactions were tested in vitro and in vivo using affinity binding and a two-hybrid analysis. We show that the self-interaction of the protein is mediated by at least two domains, corresponding to the first third of the protein (the so-called prion-forming domain) and the C-terminal catalytic domain.

SUBMITTER: Fernandez-Bellot E 

PROVIDER: S-EPMC1220066 | biostudies-other | 1999 Mar

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC3638396 | biostudies-literature
| S-EPMC5043269 | biostudies-literature
| S-EPMC5986701 | biostudies-literature
| S-EPMC8633096 | biostudies-literature
| S-EPMC5553303 | biostudies-literature
| S-EPMC6422396 | biostudies-literature
| S-EPMC4601363 | biostudies-other
| S-EPMC4383067 | biostudies-literature
| S-EPMC4074094 | biostudies-literature
| S-EPMC2733036 | biostudies-literature