Disruption of the MRP-L23 gene encoding the mitochondrial ribosomal protein L23 is lethal for Kluyveromyces lactis but not for Saccharomyces cerevisiae

2000 ◽  
Vol 37 (2) ◽  
pp. 87-93 ◽  
Author(s):  
Gerald L. Murray ◽  
Wei Guo Bao ◽  
Hiroshi Fukuhara ◽  
Xiao Ming Zuo ◽  
G. Desmond Clark-Walker ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Protein ◽  
Kluyveromyces Lactis ◽  
Gene Encoding ◽  
Mitochondrial Ribosomal Protein

scholarly journals Silencing of the Nuclear RPS10 Gene Encoding Mitochondrial Ribosomal Protein Alters Translation in Arabidopsis Mitochondria

2013 ◽  
Vol 25 (5) ◽  
pp. 1855-1867 ◽  
Author(s):  
Malgorzata Kwasniak ◽  
Pawel Majewski ◽  
Renata Skibior ◽  
Aleksandra Adamowicz ◽  
Malgorzata Czarna ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Gene Encoding ◽  
Mitochondrial Ribosomal Protein

scholarly journals Evidence that Synthesis of the Saccharomyces cerevisiae Mitochondrially Encoded Ribosomal Protein Var1p May Be Membrane Localized

2003 ◽  
Vol 2 (3) ◽  
pp. 651-653 ◽  
Author(s):  
Alessandro Fiori ◽  
Thomas L. Mason ◽  
Thomas D. Fox
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Protein ◽  
Mitochondrial Gene ◽  
Membrane Surface ◽  
Protein A ◽  
Untranslated Regions ◽  
Gene Encoding ◽  
Inner Membrane ◽  
Close Proximity ◽  
Untranslated Leaders

ABSTRACT The 5′-untranslated leaders of mitochondrial mRNAs appear to localize translation within the organelle. VAR1 is the only yeast mitochondrial gene encoding a major soluble protein. A chimeric mRNA bearing the VAR1 untranslated regions and the coding sequence for pre-Cox2p appears to be translated at the inner membrane surface. We propose that translation of the ribosomal protein Var1p is also likely to occur in close proximity to the inner membrane.

Gal80 proteins of Kluyveromyces lactis and Saccharomyces cerevisiae are highly conserved but contribute differently to glucose repression of the galactose regulon

1993 ◽  
Vol 13 (12) ◽  
pp. 7566-7576
Author(s):  
F T Zenke ◽  
W Zachariae ◽  
A Lunkes ◽  
K D Breunig
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Binding Sites ◽  
Glucose Repression ◽  
Kluyveromyces Lactis ◽  
Constitutive Expression ◽  
Indirect Evidence ◽  
Transcriptional Activator ◽  
Negative Regulator ◽  
Gene Encoding ◽  
Fold Induction

We cloned the GAL80 gene encoding the negative regulator of the transcriptional activator Gal4 (Lac9) from the yeast Kluyveromyces lactis. The deduced amino acid sequence of K. lactis GAL80 revealed a strong structural conservation between K. lactis Gal80 and the homologous Saccharomyces cerevisiae protein, with an overall identity of 60% and two conserved blocks with over 80% identical residues. K. lactis gal80 disruption mutants show constitutive expression of the lactose/galactose metabolic genes, confirming that K. lactis Gal80 functions in essentially in the same way as does S. cerevisiae Gal80, blocking activation by the transcriptional activator Lac9 (K. lactis Gal4) in the absence of an inducing sugar. However, in contrast to S. cerevisiae, in which Gal4-dependent activation is strongly inhibited by glucose even in a gal80 mutant, glucose repressibility is almost completely lost in gal80 mutants of K. lactis. Indirect evidence suggests that this difference in phenotype is due to a higher activator concentration in K. lactis which is able to overcome glucose repression. Expression of the K. lactis GAL80 gene is controlled by Lac9. Two high-affinity binding sites in the GAL80 promoter mediate a 70-fold induction by galactose and hence negative autoregulation by Gal80. Gal80 in turn not only controls Lac9 activity but also has a moderate influence on its rate of synthesis. Thus, a feedback control mechanism exists between the positive and negative regulators. By mutating the Lac9 binding sites of the GAL80 promoter, we could show that induction of GAL80 is required to prevent activation of the lactose/galactose regulon in glycerol or glucose plus galactose, whereas the noninduced level of Gal80 is sufficient to completely block Lac9 function in glucose.

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