Mss51p, a putative translational activator of cytochrome c oxidase subunit-1 ( COX1 ) mRNA, is required for synthesis of Cox1p in Saccharomyces cerevisiae

2000 ◽  
Vol 37 (4) ◽  
pp. 213-220 ◽  
Author(s):  
M. Siep ◽  
K. van Oosterum ◽  
H. Neufeglise ◽  
H. van der Spek ◽  
L. A. Grivell
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Oxidase Subunit ◽  
Translational Activator

scholarly journals Translocation and Assembly of Mitochondrially Coded Saccharomyces cerevisiae Cytochrome c Oxidase Subunit Cox2 by Oxa1 and Yme1 in the Absence of Cox18

Genetics ◽  
2009 ◽  
Vol 182 (2) ◽  
pp. 519-528 ◽  
Author(s):  
Heather L. Fiumera ◽  
Maitreya J. Dunham ◽  
Scott A. Saracco ◽  
Christine A. Butler ◽  
Jessica A. Kelly ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Oxidase Subunit

scholarly journals Release of two Saccharomyces cerevisiae cytochrome genes, COX6 and CYC1, from glucose repression requires the SNF1 and SSN6 gene products.

1990 ◽  
Vol 10 (3) ◽  
pp. 1297-1300 ◽  
Author(s):  
R M Wright ◽  
R O Poyton
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Genetic Background ◽  
Glucose Repression ◽  
Mitochondrial Proteins ◽  
Gene Products ◽  
Oxidase Subunit ◽  
Yeast Genes

We show here that SNF1 and SSN6 are required for derepression of the glucose-repressible yeast genes COX6 and CYC1, which encode the mitochondrial proteins cytochrome c oxidase subunit VI and iso-1-cytochrome c, respectively. In an snf1 mutant genetic background, the transcription of both COX6 and CYC1 continued to be repressed after cells were shifted into derepressing media. In an ssn6 mutant genetic background, both COX6 and CYC1 were expressed constitutively at high levels in repressing media. SSN6 acted epistatically to SNF1 in the regulation of both cytochrome genes. These findings are similar to previous findings on the effects of SNF1 and SSN6 on SUC2 expression in Saccharomyces cerevisiae and are consistent with a model proposing that SNF1 exerts its effect through SSN6 on COX6 and CYC1.

scholarly journals Overexpression of a leaderless form of yeast cytochrome c oxidase subunit Va circumvents the requirement for a leader peptide in mitochondrial import.

1990 ◽  
Vol 10 (9) ◽  
pp. 4984-4986 ◽  
Author(s):  
L K Dircks ◽  
R O Poyton
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Mitochondrial Protein ◽  
Leader Peptide ◽  
Mitochondrial Import ◽  
Oxidase Subunit

Subunit Va of Saccharomyces cerevisiae cytochrome c oxidase is a nucleus-encoded mitochondrial protein that is derived from a precursor with a 20-residue leader peptide. We previously reported that this leader peptide is required for import of subunit Va into mitochondria in vivo (S. M. Glaser, C. E. Trueblood, L. K. Dircks, R. O. Poyton, and M. G. Cumsky, J. Cell. Biochem. 36:275-278, 1988). Here we show that overproduction of a leaderless form of subunit Va circumvents the leader peptide requirement for import into mitochondria in vivo.

scholarly journals Differential regulation of the two genes encoding Saccharomyces cerevisiae cytochrome c oxidase subunit V by heme and the HAP2 and REO1 genes.

1988 ◽  
Vol 8 (10) ◽  
pp. 4537-4540 ◽  
Author(s):  
C E Trueblood ◽  
R M Wright ◽  
R O Poyton
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Differential Regulation ◽  
Negative Regulation ◽  
Low Oxygen ◽  
Oxidase Subunit ◽  
Low Oxygen Tension ◽  
Genes Encoding ◽  
Heme Regulation

In Saccharomyces cerevisiae, the COX5a and COX5b genes encode two forms of cytochrome c oxidase subunit V, Va and Vb. We report here that heme increases COX5a expression and decreases COX5b expression and that the HAP2 and REO1 genes are involved in positive regulation of COX5a and negative regulation of COX5b, respectively. Heme regulation of COX5a and COX5b may dictate which subunit V isoform is available for assembly into cytochrome c oxidase under conditions of high- and low-oxygen tension.

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