Abstract
The conditional ero1-1 mutant, deficient in the ER-localized PDI oxidase Ero1p, is blocked in disulfide bond formation under restrictive conditions, such as high temperature, lack of oxygen, or high concentrations of membrane-permeant thiols. Previous studies of the physiological consequences of the ero1-1 mutation were carried out in a leu2 mutant. The ero1-1 leu2 strain does not grow in standard synthetic complete medium at 30 degrees C, a defect that can be remedied by increasing the L-leucine concentration in the medium or by transforming the ero1-1 leu2 strain with the LEU2 wild-type allele. In addition, the LEU2 gene can partially complement the growth impairment at 37 degrees C of the ero1-1 leu2 mutant. The leucine transporter Bap2p exhibits a dramatic decrease in stability in an ero1-1 strain, which may account for the pronounced leucine demand observed in the ero1-1 leu2 mutant.
Udgivelsesdato: 2007-Dec
Udgivelsesdato: 2007-Dec
Originalsprog | Engelsk |
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Tidsskrift | Bioscience, Biotechnology, and Biochemistry |
Vol/bind | 71 |
Udgave nummer | 12 |
Sider (fra-til) | 2934-42 |
Antal sider | 8 |
ISSN | 0916-8451 |
Status | Udgivet - 2007 |