PET1402, a nuclear gene required for proteolytic processing of cytochrome oxidase subunit 2 in yeast - PubMed (original) (raw)
. 1994 Nov 1;245(3):272-8.
doi: 10.1007/BF00290106.
Affiliations
- PMID: 7816036
- DOI: 10.1007/BF00290106
PET1402, a nuclear gene required for proteolytic processing of cytochrome oxidase subunit 2 in yeast
M Bauer et al. Mol Gen Genet. 1994.
Abstract
The nuclear mutation pet ts1402 prevents proteolytic processing of the precursor of cytochrome oxidase subunit 2 (cox2) in Saccharomyces cerevisiae. The structural gene PET1402 was isolated by genetic complementation of the temperature-sensitive mutation. DNA sequence analysis identified a 1206-bp open reading frame, which is located 215 bp upstream of the PET122 gene. The DNA sequence of PET1402 predicts a hydrophobic, integral membrane protein with four transmembrane segments and a typical mitochondrial targeting sequence. Weak sequence similarity was found to two bacterial proteins of unknown function. Haploid cells containing a null allelle of PET1402 are respiratory deficient.
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References
- Yeast. 1989 Sep-Oct;5(5):321-403 - PubMed
- Proc Natl Acad Sci U S A. 1980 Apr;77(4):2119-23 - PubMed
- Yeast. 1986 Sep;2(3):163-7 - PubMed
- EMBO J. 1991 Feb;10(2):247-54 - PubMed
- EMBO J. 1983;2(7):1049-54 - PubMed
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