The yeast cAMP protein kinase Tpk3p is involved in the regulation of mitochondrial enzymatic content during growth (original) (raw)
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Control of growth yield of yeast on respiratory substrate by mitochondrial content
Thermochimica Acta, 2002
It is well documented that the growth yield of microorganisms depends on the fraction of ATP utilized for cell maintenance compared to that used for biomass synthesis per se. During aerobic growth, the growth yield may also be a function of the yield of ATP synthesis by oxidative phosphorylation (i.e. ATP/O ratio), a parameter which can vary in vitro according to the functional steady state of mitochondria.
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2002
The aim of this study was to investigate the effects of an overactivation of the cAMP/protein kinase A signaling pathway on the energetic metabolism of growing yeast. By using a cAMP-permeant mutant strain, we show that the rise in intracellular cAMP activates both anabolic and catabolic pathways. Indeed, different physiological patterns were observed with respect to the growth condition: (i) When cells were grown with a limiting amount of lactate, cAMP addition markedly increased the growth rate, whereas it only slightly increased the mitochondrial and cellular protein content. In parallel, the respiratory rate increased and the growth yield, as assessed by direct microcalorimetry, was not significantly modified by cAMP. (ii) Under conditions where the growth rate was already optimal (high lactate concentration), exogenous cAMP led to a proliferation of well-coupled mitochondria within cells and to an accumulation of cellular and mitochondrial proteins. This phenomenon was associated with a rise in the respiratory activity, thus leading to a drop in the growth yield. (iii) Under conditions of catabolic repression (high glucose concentration), cAMP addition markedly increased the fermentation rate and decreased the growth yield. It is concluded that overactivation of the cAMP/PKA pathway leads to uncoupling between biomass synthesis and catabolism, under conditions where an optimal growth rate is sustained by either a fermentative or a respiratory metabolism. D : S 0 0 0 5 -2 7 2 8 ( 0 2 ) 0 0 2 4 0 -2
cAMP-Dependent Protein Kinase Activity in Yeast Mitochondria
Zeitschrift für Naturforschung C, 1987
Two different cAMP-binding proteins have been identified in yeast mitochondria by photo affinity labelling and based on the occurrence of cAMP-binding activity in two different sub-mito chondrial fractions. One protein (Mr 45-46000) is tightly bound to the inner mitochondrial membrane whereas the other (Mr 42000) is found in the soluble intermembrane space. With endogenous substrate cAMP-dependent protein kinase activity could not be demonstrated with sufficient clarity. However, using acidic heterologous substrates, like casein and phosvitin, one cAMP-dependent protein kinase was identified in the intermembrane space. Only low phosphate incorporation was found using histone fractions as substrate. cAMP-dependent modification of proteins appears to be very shortlived in mitochondria. Its physiological significance remains unknown, since neither mitochondrial transcription, translation, respiration nor import of cyto-plasmically synthesized precursors into mitochondria appear to be...
Cells
Mitochondrial biogenesis is a complex process. It requires the contribution of both the nuclear and the mitochondrial genomes and therefore cross talk between the nucleus and mitochondria. Cellular energy demand can vary by great length and it is now well known that one way to adjust adenosine triphosphate (ATP) synthesis to energy demand is through modulation of mitochondrial content in eukaryotes. The knowledge of actors and signals regulating mitochondrial biogenesis is thus of high importance. Here, we review the regulation of mitochondrial biogenesis both in yeast and in mammalian cells through mitochondrial reactive oxygen species.
Activation of Ras cascade increases the mitochondrial enzyme content of respiratory competent yeast
Biochemical and Biophysical Research Communications, 2002
We investigated the effects of genetic and physiological modulations of the cAMP-protein kinase A pathway on mitochondrial biogenesis of yeast cells grown on lactate. Yeast mutants with over-activated Ras/adenylate cyclase pathway (i.e., Ras2 val19 , ira1Dira2D) or with a constitutive downstream activation of protein kinases A (i.e., bcyD) showed an increase in the mitochondrial enzyme content. In contrast, loss of Ras activity (i.e., Ras2 mutant) resulted in a slight decrease. The treatment by cAMP of a responsive mutant increased the oxidative phosphorylation capacity of cells and increased the transcript level of nuclear genes encoding for mitochondrial proteins. In contrast, the transcript level of mitochondrial DNA genes was unchanged. It is concluded that the Ras/cAMP/protein kinase A pathway is part of the regulatory circuit controlling biogenesis of the oxidative phosphorylation complexes in yeast cells. Ó
cAMP-PKA signalling to mitochondria
Cellular Signalling 17 (2005) 279–287
Energy metabolism and, specifically, the coupling of mitochondria to growth and survival is controlled by the cAMP-PKA pathway in yeast. In higher eukaryotes, cAMP signaling originating at the plasma membrane is distributed to different subcellular districts by cAMP waves received by PKA bound to PKA anchor proteins (AKAPs) tethered to these compartments. This review focuses on the subgroup of AKAPs that anchor PKA to the mitochondrial outer membrane (mtAKAPs). Only PKA anchored to mtAKAPs can efficiently transmit cAMP signals to mitochondria. mtAKAP complexes are remarkably heterogeneous. In addition to PKA regulatory subunits, they may include mRNAs, tyrosine phosphatase(s) and tyrosine kinase(s). Selective regulation of these components by cAMP-PKA integrates various signal transduction pathways and can determine which subcellular compartment receives the signal. Unveiling the interactions among the components of these large complexes will shed light on how cAMP and PKA regulate vital mitochondrial processes.
Dynamic regulation of mitochondrial respiratory chain efficiency in Saccharomyces cerevisiae
Microbiology, 2011
To adapt to changes in the environment, cells have to dynamically alter their phenotype in response to, for instance, temperature and oxygen availability. Interestingly, mitochondrial function in Saccharomyces cerevisiae is inherently temperature sensitive; above 37 6C, yeast cells cannot grow on respiratory carbon sources. To investigate this phenomenon, we studied the effect of cultivation temperature on the efficiency (production of ATP per atom of oxygen consumed, or P/O) of the yeast respiratory chain in glucose-limited chemostats. We determined that even though the specific oxygen consumption rate did not change with temperature, oxygen consumption no longer contributed to mitochondrial ATP generation at temperatures higher than 37 6C. Remarkably, between 30 and 37 6C, we observed a linear increase in respiratory efficiency with growth temperature, up to a P/O of 1.4, close to the theoretical maximum that can be reached in vivo. The temperature-dependent increase in efficiency required the presence of the mitochondrial glycerol-3-phosphate dehydrogenase GUT2. Respiratory chain efficiency was also altered in response to changes in oxygen availibility. Our data show that, even in the absence of alternative oxidases or uncoupling proteins, yeast has retained the ability to dynamically regulate the efficiency of coupling of oxygen consumption to proton translocation in the respiratory chain in response to changes in the environment.
Yeast, 1987
We describe the identification and submitochondrial localization of four protein kinases and of their target proteins in derepressed yeast mitochondria. The activity of one of the kinases depends on the presence of cyclic AMP (cAMP). It is soluble and localized in the mitochondrial intermembrane space. Its natural target is a polypeptide of 40 kDa molecular mass, which is bound to the inner membrane. Besides this natural target this kinase phosphorylates acidic heterologous proteins, like casein, with high efficiency. The other protein kinases identified so far are cAMP-independent. At least one is localized in the matrix having its natural substrates (49 and 24 kDa) in the same compartment. Two others are firmly bound to the inner membrane phosphorylating target proteins in the inner membrane (52-5 kDa) and in the intermembrane space (17-5 kDa), respectively.