Mitochondrial Genetics in a Petite-Negative Yeast

Schäfer, Bernd; Wolf, Klaus

doi:10.1007/978-3-662-10360-9_28

Cited by 3 publications

(3 citation statements)

References 42 publications

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“…It is shown that, as in budding yeast (22), the NTD of Cdc17 is suf®cient to target GFP to both the nucleus and mitochondria, consistent with a model in which the use of alternate in-frame start codons results in the production of distinct nuclear and mitochondrial forms of the Cdc17 protein. Mitochondrial function is known to be essential for ®ssion yeast viability (26). Here it is shown that co-expression of nuclear and mitochondrial forms in vivo restores full viability to cdc17D cells, whereas expression of either protein alone does not.…”

Section: Introductionmentioning

confidence: 82%

Functional analysis of subcellular localization and protein-protein interaction sequences in the essential DNA ligase I protein of fission yeast

Martin¹

2004

Nucleic Acids Research

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DNA ligase I (Lig I) has key roles in chromosomal DNA replication and repair in the eukaryotic cell nucleus. In the budding yeast Saccharomyces cerevisiae the Lig I enzyme Cdc9p is also required for mitochondrial DNA replication and repair. In this report, dual nuclear-mitochondrial localization is demonstrated to be a property of the essential Lig I enzyme Cdc17 from the distantly related fission yeast Schizosaccharomyces pombe. Expression of nuclear and mitochondrial forms of Cdc17 from separate genes shows that, whereas expression of either protein alone is insufficient to restore viability to cells lacking endogenous Cdc17, co-expression restores full viability. In the nucleus, Lig I interacts with the sliding clamp proliferating cell nuclear antigen (PCNA) via a conserved PCNA interacting sequence motif known as a PIP box. Deletion of the PIP motif from the N-terminus of the nuclear form of Cdc17 fails to abolish Cdc17 function, indicating that PCNA binding by Cdc17 is not an absolute requirement for completion of S-phase.

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Section: Introductionmentioning

confidence: 82%

Functional analysis of subcellular localization and protein-protein interaction sequences in the essential DNA ligase I protein of fission yeast

Martin¹

2004

Nucleic Acids Research

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“…Nevertheless in fission yeast, the Crabtree effect is less pronounced than in S. cerevisiae since the inhibition of oxygen consumption by glucose is smaller; in other words S. pombe maintains a higher respiration rate in the presence of glucose [22] . Consistently, it is hard to isolate respiratory-deficient cells ( petite ) in S. pombe [23] , [24] , while these mutants occur spontaneously in S. cerevisiae . Furthermore, S. pombe differs from S. cerevisiae because of its lack of glyoxylate cycle that makes it inefficient in ethanol consumption as carbon source [25] , [26] .…”

Section: Introductionmentioning

confidence: 99%

Pro-Aging Effects of Glucose Signaling through a G Protein-Coupled Glucose Receptor in Fission Yeast

et al. 2009

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Glucose is the preferred carbon and energy source in prokaryotes, unicellular eukaryotes, and metazoans. However, excess of glucose has been associated with several diseases, including diabetes and the less understood process of aging. On the contrary, limiting glucose (i.e., calorie restriction) slows aging and age-related diseases in most species. Understanding the mechanism by which glucose limits life span is therefore important for any attempt to control aging and age-related diseases. Here, we use the yeast Schizosaccharomyces pombe as a model to study the regulation of chronological life span by glucose. Growth of S. pombe at a reduced concentration of glucose increased life span and oxidative stress resistance as reported before for many other organisms. Surprisingly, loss of the Git3 glucose receptor, a G protein-coupled receptor, also increased life span in conditions where glucose consumption was not affected. These results suggest a role for glucose-signaling pathways in life span regulation. In agreement, constitutive activation of the Gα subunit acting downstream of Git3 accelerated aging in S. pombe and inhibited the effects of calorie restriction. A similar pro-aging effect of glucose was documented in mutants of hexokinase, which cannot metabolize glucose and, therefore, are exposed to constitutive glucose signaling. The pro-aging effect of glucose signaling on life span correlated with an increase in reactive oxygen species and a decrease in oxidative stress resistance and respiration rate. Likewise, the anti-aging effect of both calorie restriction and the Δgit3 mutation was accompanied by increased respiration and lower reactive oxygen species production. Altogether, our data suggest an important role for glucose signaling through the Git3/PKA pathway to regulate S. pombe life span.

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“…Lastly, naturally occurring strains of Sz. pombe are petite ‐negative, unable to survive without mtDNA (Schäfer and Wolf, ). It remains unknown what the effect of Sp Mdm31 loss on stability of mtDNA in Sz.…”

Section: Introductionmentioning

confidence: 99%

Mdm31 protein mediates sensitivity to potassium ionophores but does not regulate mitochondrial morphology or phospholipid trafficking inSchizosaccharomyces pombe

Ivan

Lajdova

Abelovska

et al. 2015

Yeast

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Mdm31p is an inner mitochondrial membrane (IMM) protein with unknown function in Saccharomyces cerevisiae. Mutants lacking Mdm31p contain only a few giant spherical mitochondria with disorganized internal structure, altered phospholipid composition and disturbed ion homeostasis, accompanied by increased resistance to the electroneutral K + /H + ionophore nigericin. These phenotypes are interpreted as resulting from diverse roles of Mdm31p, presumably in linking mitochondrial DNA (mtDNA) to the machinery involved in segregation of mitochondria, in mediating cation transport across IMM and in phospholipid shuttling between mitochondrial membranes. To investigate which of the roles of Mdm31p are conserved in ascomycetous yeasts, we analysed the Mdm31p orthologue in Schizosaccharomyces pombe. Our results demonstrate that, similarly to its S. cerevisiae counterpart, SpMdm31 is a mitochondrial protein and its absence results in increased resistance to nigericin. However, in contrast to S. cerevisiae, Sz. pombe cells lacking SpMdm31 are also less sensitive to the electrogenic K + ionophore valinomycin. Moreover, mitochondria of the fission yeast mdm31Δ mutant display no changes in morphology or phospholipid composition. Therefore, in terms of function, the two orthologous proteins appear to have considerably diverged between these two evolutionarily distant yeast species, possibly sharing only their participation in ion homeostasis.

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Mitochondrial Genetics in a Petite-Negative Yeast

Cited by 3 publications

References 42 publications

Functional analysis of subcellular localization and protein-protein interaction sequences in the essential DNA ligase I protein of fission yeast

Functional analysis of subcellular localization and protein-protein interaction sequences in the essential DNA ligase I protein of fission yeast

Pro-Aging Effects of Glucose Signaling through a G Protein-Coupled Glucose Receptor in Fission Yeast

Mdm31 protein mediates sensitivity to potassium ionophores but does not regulate mitochondrial morphology or phospholipid trafficking inSchizosaccharomyces pombe

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