Abstract
SHY1 codes for a mitochondrial protein required for full expression of cytochrome oxidase (COX) in Saccharomyces cerevisiae. Mutations in the homologous human gene (SURF1) have been reported to cause Leigh's syndrome, a neurological disease associated with COX deficiency. The function of Shy1p/ Surf1p is poorly understood. Here we have characterized revertants of shy1 null mutants carrying extragenic nuclear suppressor mutations. The steady-state levels of COX in the revertants is increased by a factor of 4-5, accounting for their ability to respire and grow on non-fermentable carbon sources at nearly wild-type rates. The suppressor mutations are in MSS51, a gene previously implicated in processing and translation of the COX1 transcript for subunit 1 (Cox1) of COX. The function of Shy1p and the mechanism of suppression of shy1 mutants were examined by comparing the rates of synthesis and turnover of the mitochondrial translation products in wild-type, mutant and revertant cells. We propose that Shy1p promotes the formation of an assembly intermediate in which Cox1 is one of the partners.
Original language | English (US) |
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Pages (from-to) | 43-52 |
Number of pages | 10 |
Journal | EMBO Journal |
Volume | 21 |
Issue number | 1-2 |
DOIs | |
State | Published - Jan 15 2002 |
Externally published | Yes |
Keywords
- Cytochrome oxidase
- Leigh's syndrome
- MSS51
- SHY1
- SURF1
ASJC Scopus subject areas
- Genetics
- Cell Biology