Characterization of a cyclic AMP-binding protein from bakers' yeast. Identification as a regulatory subunit of cyclic AMP-dependent protein kinase.

Hixson, Craig S.; Krebs, Edwin G.

doi:10.1016/s0021-9258(19)86004-0

Cited by 107 publications

(14 citation statements)

References 53 publications

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“…Inactive PKA consists of two catalytical subunits (combinations of Tpk1p/2p/3p) that are being inhibited by two Bcy1p subunits [157]. As cAMP levels increase after signaling from Gpr1p and/or Ras1p/2p, cAMP promotes the autophosphorylation of the Tpk subunits (by a yet to be elucidated mechanism) which leads to their dissociation from the regulatory Bcy1p subunits, and the activation of PKA [157][158][159].…”

Section: Targets Induced/activated By Active Pkamentioning

confidence: 99%

D-Xylose Sensing in Saccharomyces cerevisiae: Insights from D-Glucose Signaling and Native D-Xylose Utilizers

Brink

Borgström

Persson

et al. 2021

IJMS

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Extension of the substrate range is among one of the metabolic engineering goals for microorganisms used in biotechnological processes because it enables the use of a wide range of raw materials as substrates. One of the most prominent examples is the engineering of baker’s yeast Saccharomyces cerevisiae for the utilization of d-xylose, a five-carbon sugar found in high abundance in lignocellulosic biomass and a key substrate to achieve good process economy in chemical production from renewable and non-edible plant feedstocks. Despite many excellent engineering strategies that have allowed recombinant S. cerevisiae to ferment d-xylose to ethanol at high yields, the consumption rate of d-xylose is still significantly lower than that of its preferred sugar d-glucose. In mixed d-glucose/d-xylose cultivations, d-xylose is only utilized after d-glucose depletion, which leads to prolonged process times and added costs. Due to this limitation, the response on d-xylose in the native sugar signaling pathways has emerged as a promising next-level engineering target. Here we review the current status of the knowledge of the response of S. cerevisiae signaling pathways to d-xylose. To do this, we first summarize the response of the native sensing and signaling pathways in S. cerevisiae to d-glucose (the preferred sugar of the yeast). Using the d-glucose case as a point of reference, we then proceed to discuss the known signaling response to d-xylose in S. cerevisiae and current attempts of improving the response by signaling engineering using native targets and synthetic (non-native) regulatory circuits.

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Section: Targets Induced/activated By Active Pkamentioning

confidence: 99%

D-Xylose Sensing in Saccharomyces cerevisiae: Insights from D-Glucose Signaling and Native D-Xylose Utilizers

Brink

Borgström

Persson

et al. 2021

IJMS

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“…a single type of high-affinity binding site for cAMP as the ligand. The dissociation constant, derived from the slope of the plot, Kd = 5.9 ± 0.7 nM, is about 1 order of magnitude higher than the one reported for the cytosolic R subunit from yeast (Hixson & Krebs, 1980;Johnson et al, 1987). The concentration of binding sites calculated from the intercept of the abscissa is 1.34 pmol/mg of plasma membrane protein.…”

Section: Resultsmentioning

confidence: 54%

“…Our plasmalemma preparation is significantly deprived of both soluble and membrane-bound mitochondrial marker enzymes and concomitantly enriched in adenylate cyclase activity. Second, the size of the two membrane-associated cAMP-binding proteins differs markedly [plasma membrane 54 kDa, mitochondria 46 kDa; the soluble cytosolic cAMP-binding R subunit of yeast protein kinase A has a molecular mass of 51 kDa for comparison (Hixson & Krebs, 1980;Wingender-Drissen, 1983)]. Third, only the plasma membrane cAMP receptor is extensively Nglycosylated, which is consistent with its periplasmic orientation, whereas mitochondria lack a glycosyltransferase system.…”

Section: Discussionmentioning

confidence: 99%

A cAMP-binding ectoprotein in the yeast Saccharomyces cerevisiae

Müller

Bandlow²

1991

Biochemistry

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Purified plasma membranes from the yeast Saccharomyces cerevisiae bind about 1.2 pmol of cAMP/mg of protein with high affinity (Kd = 6 nM). By using photoaffinity labeling with 8-N3-[32P]cAMP, we have identified in plasma membrane vesicles a CAMP-binding protein (M, = 54 000) that is present also in bcyl disruption mutants, lacking the cytoplasmic R subunit of protein kinase A (PKA). This argues that it is genetically unrelated to PKA. Neither high salt, nor alkaline carbonate, nor CAMP extract the protein from the membrane, suggesting that it is not peripherally bound. The observation that (glycosy1)phosphatidylinositol-specific phospholipases (or nitrous acid) release the amphiphilic protein from the membrane, thereby converting it to a hydrophilic form, indicates anchorage by a glycolipidic membrane anchor. Treatment with N-glycanase reduces the M, to 44000-46000 indicative of a modification by N-linked carbohydrate side chain(s). In addition to the action of a phospholipase, the efficient release from the membrane requires the removal of the carbohydrate side chain(s) or the presence of high salt or methyl a-mannopyranoside, suggesting complex interactions with the membrane involving not only the glycolipidic anchor but also the glycan side chain(s). Topological studies show that the protein is exposed to the periplasmic space, raising intriguing questions for the function of this protein.

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“…BCY1 , the gene encoding the regulatory subunit for cAMP-dependent PKA, is located on this chromosome. In the absence of cAMP, Bcy1 inhibits PKA ( Hixson and Krebs, 1980 ; Toda et al, 1987 ). Overexpression of BCY1 is linked to reduced PKA activity which leads to a decrease in Nth1 activity and results in greater trehalose accumulation and increased thermotolerance ( Portela et al, 2003 ).…”

Section: Discussionmentioning

confidence: 99%

Kveik Brewing Yeasts Demonstrate Wide Flexibility in Beer Fermentation Temperature Tolerance and Exhibit Enhanced Trehalose Accumulation

et al. 2022

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Traditional Norwegian Farmhouse ale yeasts, also known as kveik, have captured the attention of the brewing community in recent years. Kveik were recently reported as fast fermenting thermo- and ethanol tolerant yeasts with the capacity to produce a variety of interesting flavor metabolites. They are a genetically distinct group of domesticated beer yeasts of admixed origin with one parent from the “Beer 1” clade and the other unknown. While kveik are known to ferment wort efficiently at warmer temperatures, their range of fermentation temperatures and corresponding fermentation efficiencies, remain uncharacterized. In addition, the characteristics responsible for their increased thermotolerance remain largely unknown. Here we demonstrate variation in kveik strains at a wide range of fermentation temperatures and show not all kveik strains are equal in fermentation performance and stress tolerance. Furthermore, we uncovered an increased capacity of kveik strains to accumulate intracellular trehalose, which likely contributes to their increased thermo- and ethanol tolerances. Taken together our results present a clearer picture of the future opportunities presented by Norwegian kveik yeasts and offer further insight into their applications in brewing.

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Characterization of a cyclic AMP-binding protein from bakers' yeast. Identification as a regulatory subunit of cyclic AMP-dependent protein kinase.

Cited by 107 publications

References 53 publications

D-Xylose Sensing in Saccharomyces cerevisiae: Insights from D-Glucose Signaling and Native D-Xylose Utilizers

D-Xylose Sensing in Saccharomyces cerevisiae: Insights from D-Glucose Signaling and Native D-Xylose Utilizers

A cAMP-binding ectoprotein in the yeast Saccharomyces cerevisiae

Kveik Brewing Yeasts Demonstrate Wide Flexibility in Beer Fermentation Temperature Tolerance and Exhibit Enhanced Trehalose Accumulation

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