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PubMedDate not supplied

Enumeration of total yeasts and molds in foods by the SimPlate Yeast and Mold-Color Indicator method and conventional culture methods: collaborative study.

The relative effectiveness of the SimPlate Yeast and Mold-Color Indicator method (Y&M-CI) was compared to the U.S. Food and Drug Administration's (FDA) Bacteriological Analytical Manual (BAM) method and the proposed International Organization for Standardization (ISO) method, ISO/CD 21527, for enumerating yeasts and molds in foods. Test portions were prepared and incubated according to the conditions stated in both the BAM and ISO methods. Six food types were analyzed: frozen corn dogs, nut meats, frozen fruits, cake mix, cereal, and fresh cheese. Nut meats, frozen fruits, and fresh cheese were naturally contaminated. All other foods were artificially contaminated with either a yeast or mold. Seventeen laboratories throughout North America and Europe participated in the study. Three method comparisons were conducted. In general, there was <0.3 mean log count difference in recovery between the SimPlate method and the 2 corresponding reference methods. Moreover, mean log counts between the 2 reference methods were also very similar. The repeatability (Sr) and reproducibility (SR) standard deviations were comparable between the 3 method comparisons. These results indicate that the BAM method and the SimPlate method are equivalent for enumerating yeast and mold populations in foods. Similarly, the SimPlate method is comparable to the proposed ISO method when test portions are prepared and incubated as defined in the proposed ISO method.

Colony Count, Microbial↗
PubMed1998

Construction of poly-met DNA yeast hybrids for increased methionine content: technofunctional properties of the hybrid yeasts.

Methionine is a limiting essential amino acid in human nutrition, to overcome the possible overdosage and improve bioavailability methionine supply should be in protein bound form. So insertion a poly-met encoding DNA sequence results a more efficient solution in increasing methionine content of yeast. Poly-met DNA yeast hybrids were constructed of Saccharomyces cerevisiae CB89, an auxotrophic mutant strain. Synthetic DNA sequence encoding methionine polypeptide was inserted into the polylinker region of pVT-U 100 vector with 2 mu plasmid replicon. After transformation of E. coli HB101 cells the efficiency of the ligation and transformation was checked by digesting the minipreps. S. cerevisiae CB89 was transformed with vector-poly-met insert and with the plasmid vector only as well. Hybrid yeasts were selected on uracilless medium. PVT-U 100 can be used as vector for the expression of DNA sequence in S. cerevisiae. The vector harbours the promoter of ADC1 gene immediately downstream from the promoter lies a polylinker sequence comprising unique restriction enzyme sites for BamHI, HindIII, PvuII, SacI, Xhol. The polylinker sequence is followed by the transcriptional stop site and polyadenylation signal of ADC1 gene. Plasmid pVT-U 100 has selection markers for S. cerevisiae (URA3) and for E. coli (amp, per F). Results show that the poly-met DNA hybrids methionine content is influenced by the length of the insert. Fusion hybrids containing 600 bp oligo insert showed the best values. Distribution of methionine content in the protein subfractions of polymet DNA hybrid and parent strain CB89 was determined in dependence of glucose concentration and aeration intensity. The increase in synthesized methionine appeared in fractions 1 + 2 and residue. Technofunctional properties of parent strains and hybrids were compared for whole cells and cell wall (residue). Results demonstrate that enrichment in methionine in the cell wall fraction resulted improvement of emulsifying ability. Bioavailability of methionine content was better in DNA hybrid yeast than in parent strain and was the best when propagated in whey medium.

Culture Media↗
PubMed1995

Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including the Tyl-H3 retrotransposon, the suf1(+) frameshift suppressor gene for tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.

We have sequenced on both strands a 44,019 bp fragment located on the left arm of Saccharomyces cerevisiae chromosome XV. The sequenced segment contains 22 open reading frames (ORFs) of at least 100 amino acids long, one of which probably contains an intron. Six of the 22 ORFs correspond to known proteins: the multicopy suppressor of Snf1 protein 1, the two Tyl-H3 transposon proteins TyA and TyB, the myo-inositol transporter 2, the transcription factor protein Ino4 and the 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase. Of the 16 remaining ORFs, two show highest homologies with the yeast serine/threonine protein kinase Ste20 and the human tryptophanyl-tRNA synthetase. Eight ORFs show slight similarities with protein sequences described in data banks. DNA sequence comparison reveals also the presence of three known sequences: the Tyl-H3 transposable element, the yeast suf1(+) frameshift suppressor gene for tRNA-Gly and the yeast transfer RNA-Thr-1a. A fourth DNA sequence shows striking identities with the yeast delta elements.

Amino Acid Sequence↗
PubMed1993

Mating of the fission yeast occurs independently of pmd1+ gene product, a structural homologue of budding yeast STE6 and mammalian P-glycoproteins.

The pmd1+, a multidrug resistance gene of the fission yeast Schizosaccharomyces pombe, encodes a protein similar to the budding yeast Saccharomyces cerevisiae STE6 gene product and mammalian P-glycoproteins. The STE6 protein is a membrane transporter of a-factor, a mating pheromone of a-type S. cerevisiae, which is structurally related to M-factor of the fission yeast. However, heterothallic or homothallic pmd1 null mutant cells of S. pombe, which were constructed by means of gene disruption, showed no significant decrease in the mating abilities. On the other hand, the multidrug resistance conferred by the pmd1+ was overcome by the treatment with verapamil, a typical inhibitor of mammalian P-glycoproteins. These results indicate that the pmd1+ gene product is functionally similar to mammalian P-glycoproteins, rather than to the budding yeast STE6.

ATP Binding Cassette Transporter, Subfamily B, Mem↗
PubMed1994

The 20S proteasome mediates the degradation of mouse and yeast ornithine decarboxylase in yeast cells.

Ornithine decarboxylase (ODC), a key enzyme in the biosynthesis of polyamines, is one of the most rapidly degraded proteins in mammalian cells. Recently it has been demonstrated that mammalian ODC is degraded in vitro by the 26S protease that contains the 20S proteasome as its catalytic core, in a reaction that does not require ubiquitin. Here, we show that yeast and mouse ODC are both rapidly degraded in yeast cells and that their degradation severely inhibited in a mutant yeast cell line defective in the chymotryptic activity of proteinase yscE, the yeast 20S proteasome. These results provide compelling genetic support to previous biochemical studies suggesting the involvement of the 20S proteasome in the degradation of ornithine decarboxylase.

Animals↗
PubMed1993

Species-specific differences in covalently crosslinked complexes of yeast cytochrome c peroxidase with horse and yeast iso-1 ferricytochromes c.

1. The results of chemically crosslinking yeast cytochrome c peroxidase with both horse and yeast iso-1 ferricytochromes c have been studied by a combination of gel electrophoresis and proton NMR spectroscopy. 2. The complexes were formed at a variety of potassium phosphate concentrations ranging from 10 to 300 mM using the water soluble crosslinking agent, EDC (1-ethyl-3-[3-(dimethylamino)propyl]-carbodiimide). 3. The primary crosslinking product in both cases is the 1:1 covalent complex, but, for each pair of partner proteins the yield of the 1:1 crosslinked complex varies with the salt concentration. 4. Furthermore, at low salt concentrations the yield of the 1:1 covalent complex involving horse cytochrome c is much larger than the yield of the 1:1 covalent complex formed with yeast iso-1 cytochrome c, whereas at high salt concentrations the situation is reversed. 5. Proton NMR spectroscopy, in combination with gel electrophoresis, provides evidence for the formation of different types of 1:1 complexes for the peroxidase/yeast cytochrome c pair and has been used to study the effect of changes in the solution ionic strength upon both the peroxidases/horse cytochrome c and the peroxidase/yeast cytochrome c complexes. 6. This work indicates that electrostatic interactions between proteins play a dominant role in formation of complexes between cytochrome c peroxidase and horse ferricytochrome c, whereas the hydrophobic effect plays a comparatively larger role in stabilizing complexes between cytochrome c peroxidase and yeast iso-1 ferricytochrome c.

Animals↗
PubMed1985

Yeast tRNAAsp tertiary structure in solution and areas of interaction of the tRNA with aspartyl-tRNA synthetase. A comparative study of the yeast phenylalanine system by phosphate alkylation experiments with ethylnitrosourea.

Ethylnitrosourea is an alkylating reagent preferentially modifying phosphate groups in nucleic acids. It was used to monitor the tertiary structure, in solution, of yeast tRNAAsp and to determine those phosphate groups in contact with the cognate aspartyl-tRNA synthetase. Experiments involve 3' or 5'-end-labelled tRNA molecules, low yield modification of the free or complexed nucleic acid and specific splitting at the modified phosphate groups. The resulting end-labelled oligonucleotides are resolved on polyacrylamide sequencing gels and data analysed by autoradiography and densitometry. Experiments were conducted in parallel on yeast tRNAAsp and on tRNAPhe. In that way it was possible to compare the solution structure of two elongator tRNAs and to interpret the modification data using the known crystal structures of both tRNAs. Mapping of the phosphates in free tRNAAsp and tRNAPhe allowed the detection of differential reactivities for phosphates 8, 18, 19, 20, 22, 23, 24 and 49: phosphates 18, 19, 23, 24 and 49 are more reactive in tRNAAsp, while phosphates 8, 20 and 22 are more reactive in tRNAPhe. All other phosphates display similar reactivities in both tRNAs, in particular phosphate 60 in the T-loop, which is strongly protected. Most of these data are explained by the crystal structures of the tRNAs. Thermal transitions in tRNAAsp could be followed by chemical modifications of phosphates. Results indicate that the D-arm is more flexible than the T-loop. The phosphates in yeast tRNAAsp in contact with aspartyl-tRNA synthetase are essentially contained in three continuous stretches, including those at the corner of the amino acid accepting and D-arm, at the 5' side of the acceptor stem and in the variable loop. When represented in the three-dimensional structure of the tRNAAsp, it clearly appears that one side of the L-shaped tRNA molecule, that comprising the variable loop, is in contact with aspartyl-tRNA synthetase. In yeast tRNAPhe interacting with phenylalanyl-tRNA synthetase, the distribution of protected phosphates is different, although phosphates in the anticodon stem and variable loop are involved in both systems. With tRNAPhe, the data cannot be accommodated by the interaction model found for tRNAAsp, but they are consistent with the diagonal side model proposed by Rich & Schimmel (1977). The existence of different interaction schemes between tRNAs and aminoacyl-tRNA synthetases, correlated with the oligomeric structure of the enzyme, is proposed.

Alkylation↗
PubMed1987

Interaction of ribosomal proteins L25 from yeast and EL23 from E. coli with yeast 26S and mouse 28S rRNA.

The interaction of ribosomal protein EL23 from E. coli and L25 from yeast with yeast 26S rRNA was analysed by nitrocellulose filter binding and RNase protection experiments using both intact rRNA and various fragments prepared by in vitro transcription of cloned yeast rDNA regions in the SP6 system. The results show that EL23 efficiently and specifically interacts with the region of 26S rRNA previously identified as the binding site for the yeast ribosomal protein L25. A comparison of the oligonucleotides resulting from limited RNase T1 digestion of the heterologous EL23/26S rRNA complex with those obtained by the same treatment of the homologous L25/26S rRNA complex showed that the molecular details of the two r-protein/rRNA interactions are highly similar if not identical. Using the synthetic 26S rRNA fragments we could demonstrate that all information for the formation of a biologically active binding site is located within the region of the rRNA delimited by the sequences protected by L25 against RNase T1 digestion. Part of the sequence at the 3' end of the 5'-distal protected region, however, was found not to be essential for r-protein binding although it does enhance the efficiency of this binding. Binding experiments using synthetic mouse 28S rRNA fragments showed that neither EL23 nor L25 interact with the structural equivalent of their respective cognate binding sites present in this mammalian rRNA. We argue that the structure of the expansion sequence present in this region of mouse 28S rRNA is a major cause of this failure.

Amino Acid Sequence↗
PubMed1980

Transcriptional and translational expression of a chimeric bacterial-yeast plasmid in yeasts.

Chimeric plasmids composed of the bacterial plasmid pBR322, 2 micron yeast plasmid fragments and the 1.1 kb ura3+ fragment of yeast chromosomal DNA which codes for orotidine-5'-phosphate (OMP) decarboxylase were constructed and used to transform Escherichia coli and Saccharomyces cerevisiae recipient cells. The expression in yeast of one such plasmid was studied and compared to the expression of a chromosomally integrated bacterial plasmid. In the strain carrying the chimeric plasmid the level of OMP decarboxylase activity is about 25 times that found in either the wild-type strain or in the strain carrying the chromosomally integrated plasmid. The ampicillin gene of pBR322 is expressed in yeast. Labeling kinetics of RNA and measurements of the polyadenylated fractions showed that RNA hybridizing to the pBR322 plasmid was polyadenylated to the same extent as RNA hybridizing to the ura3+ gene. Half-lives of 10 and 20 min were estimated for the ura3+ and pBR322 transcripts respectively.

Chimera↗
PubMed1997

The correlation between adhesion of schizophyllan to yeast glucan and its effect on regeneration of yeast protoplast.

Schizophyllan, a water-soluble (1-->3)-beta-D-glucan with a triple-helical conformation, adheres to yeast glucan and curdlan gel. As the molecular weight of schizophyllan decreases, both its adhesion to the water-insoluble glucans and its ability to promote the regeneration of yeast protoplasts are reduced. Therefore, we hypothesize that schizophyllan can surround yeast protoplasts by adhering to a fragment of yeast glucan remaining or/and resynthesized on the cell surface and that this encapsulation allows regeneration of the protoplast cells to occur at very high frequency.

Carbohydrate Conformation↗
PubMed2000

The human homologue of the yeast mitochondrial AAA metalloprotease Yme1p complements a yeast yme1 disruptant.

In yeast, three AAA superfamily metalloproteases (Yme1p, Afg3p and Rca1p) are localized to the mitochondrial inner membrane where they perform roles in the assembly and turnover of the respiratory chain complexes. We have investigated the function of the proposed human orthologue of yeast Yme1p, encoded by the YME1L gene on chromosome 10p. Transfection of both HEK-293EBNA and yeast cells with a green fluorescent protein-tagged YME1L cDNA confirmed mitochondrial targeting. When expressed in a yme1 disruptant yeast strain, YME1L restored growth on glycerol at 37 degrees C. We propose that YME1L plays a phylogenetically conserved role in mitochondrial protein metabolism and could be involved in mitochondrial pathologies.

ATP-Dependent Proteases↗
PubMed1998

Identification of a possible MAP kinase cascade in Arabidopsis thaliana based on pairwise yeast two-hybrid analysis and functional complementation tests of yeast mutants.

A possible MAP kinase (MAPK) cascade of Arabidopsis thaliana was identified on the basis of both yeast 2-hybrid analysis and complementation analysis of yeast mutants. Specific protein-protein interactions between ATMPK4 (a MAPK) and MEK1 (a MAPKK) and interactions between MEK1 and ATMEKK1 (a MAPKKK) were detected by using the 2-hybrid system. A growth defect of the yeast mpk1delta mutant was reversed by coexpression of ATMPK4 and MEK1. Coexpression of the N-terminal deletion form of ATMEKK1 increased the ability of MEK1 to suppress a growth defect of the yeast pbs2delta mutant. These results suggest that ATMPK4, MEK1, and ATMEKK1 may interact with each other and constitute a specific MAPK cascade in Arabidopsis. This is the first demonstration of a possible MAPK cascade in plants.

Arabidopsis↗
PubMed1999

Cloning, characterisation, and functional expression of the Mus musculus SKD1 gene in yeast demonstrates that the mouse SKD1 and the yeast VPS4 genes are orthologues and involved in intracellular protein trafficking.

The mouse SKD1 protein displays a high degree of sequence identity (62%) to the yeast Vps4 protein, which is involved in the transport of proteins out of a prevacuolar/endosomal compartment. We isolated the mouse SKD1 locus and found that the SKD1 gene is split into 11 exons covering a region of 29kb of the genome. Interestingly, the exon/intron structure reflects to a certain degree the proposed domain structure of the protein, since the 5' located coiled-coil region and the AAA domain are flanked by introns. Analysis of the promoter region, which revealed features common for 'housekeeping genes', is consistent with previous results of a mouse multi-tissue Northern blot, confirming that SKD1 is a ubiquitously expressed gene. Expression of the full-length SKD1 cDNA in a vps4 disrupted yeast strain suppressed the temperature-sensitive growth defect of the vps4 mutant strain. Overexpression of wild type and expression of mutant Vps4 and SKD1 proteins, harbouring single amino acid exchanges in their AAA domains, induced a dominant-negative vacuolar protein sorting defect in wild type yeast cells, indicating that mouse SKD1 protein and yeast Vps4p fulfil similar functions.

ATPases Associated with Diverse Cellular Activitie↗
PubMed1992

Recognition of yeast tRNA(Phe) by its cognate yeast phenylalanyl-tRNA synthetase: an analysis of specificity.

A kinetic analysis of aminoacylation of mutant yeast tRNA(Phe) transcripts by its cognate yeast phenylalanyl-tRNA synthetase (FRS) reveals five nucleotides in tRNA(Phe) as major recognition sites for FRS. The aminoacylation kinetics for two double mutants suggest that each of the five recognition sites contributes independently to kcat/KM. Measured kinetic values for the mutants presented here and those reported previously were then used to calculate the predicted kcat/KM of misacylation for a number of noncognate tRNAs. The predicted kcat/KM values are consistent with values measured by other investigators and thus support the five-nucleotide recognition model. The kcat/KM of misacylation for all known yeast tRNAs has been calculated on the basis of this model, and the specificity of FRS for tRNA(Phe) in yeast is discussed.

Base Sequence↗
PubMed1999

Optimized expression and catalytic properties of a wheat obtusifoliol 14alpha-demethylase (CYP51) expressed in yeast. Complementation of erg11Delta yeast mutants by plant CYP51.

CYP51s form the only family of P450 proteins conserved in evolution from prokaryotes to fungi, plants and mammals. In all eukaryotes, CYP51s catalyse 14alpha-demethylation of sterols. We have recently isolated two CYP51 cDNAs from sorghum [Bak, S., Kahn, R.A., Olsen, C. E. & Halkier, B.A. (1997) Plant J. 11, 191-201] and wheat [Cabello-Hurtado, F., Zimmerlin, A., Rahier, A., Taton, M., DeRose, R., Nedelkina, S., Batard, Y., Durst, F., Pallett, K.E. & Werck-Reichhart, D. (1997) Biophys. Biochem. Res. Commun. 230, 381-385]. Wheat and sorghum CYP51 proteins show a high identity (92%) compared with their identity with their fungal and mammalian orthologues (32-39%). Data obtained with plant microsomes have previously suggested that differences in primary sequences reflect differences in sterol pathways and CYP51 substrate specificities between animals, fungi and plants. To investigate more thoroughly the properties of the plant CYP51, the wheat enzyme was expressed in yeast strains overexpressing different P450 reductases as a fusion with either yeast or plant (sorghum) membrane targeting sequences. The endogenous sterol demethylase gene (ERG11) was then disrupted. A sorghum-wheat fusion protein expressed with the Arabidopsis thaliana reductase ATR1 showed the highest level of expression and activity. The expression induced a marked proliferation of microsomal membranes so as to obtain 70 nmol P450.(L culture)-1, with CYP51 representing 1.5% of microsomal protein. Without disruption of the ERG11 gene, the expression level was fivefold reduced. CYP51 from wheat complemented the ERG11 disruption, as the modified yeasts did not need supplementation with exogenous ergosterol and grew normally under aerobic conditions. The fusion plant enzyme catalysed 14alpha-demethylation of obtusifoliol very actively (Km,app = 197 microm, kcat = 1.2 min-1) and with very strict substrate specificity. No metabolism of lanosterol and eburicol, the substrates of the fungal and mammalian CYP51s, nor metabolism of herbicides and fatty acids was detected in the recombinant yeast microsomes. Surprisingly lanosterol (Ks = 2.2 microM) and eburicol (Ks = 2.5 microm) were found to bind the active site of the plant enzyme with affinities higher than that for obtusifoliol (Ks = 289 microM), giving typical type-I spectra. The amplitudes of these spectra, however, suggested that lanosterol and eburicol were less favourably positioned to be metabolized than obtusifoliol. The recombinant enzyme was also used to test the relative binding constants of two azole compounds, LAB170250F and gamma-ketotriazole, which were previously reported to be potent inhibitors of the plant enzyme. The Ks of plant CYP51 for LAB170250F (0.29 microM) and gamma-ketotriazole (0.40 microM) calculated from the type-II sp2 nitrogen-binding spectra were in better agreement with their reported effects as plant CYP51 inhibitors than values previously determined with plant microsomes. This optimized expression system thus provides an excellent tool for detailed enzymological and mechanistic studies, and for improving the selectivity of inhibitory molecules.

Amino Acid Sequence↗
PubMed1993

Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase.

Copper-zinc superoxide dismutase catalyzes the disproportionation of superoxide anion to hydrogen peroxide and dioxygen and is thought to play an important role in protecting cells from oxygen toxicity. Saccharomyces cerevisiae strains lacking copper-zinc superoxide dismutase, which is encoded by the SOD1 gene, are sensitive to oxidative stress and exhibit a variety of growth defects including hypersensitivity to dioxygen and to superoxide-generating drugs such as paraquat. We have found that in addition to these known phenotypes, SOD1-deletion strains fail to grow on agar containing the respiratory carbon source lactate. We demonstrate here that expression of the yeast or monkey metallothionein proteins in the presence of copper suppresses the lactate growth defect and some other phenotypes associated with SOD1-deletion strains, indicating that copper metallothioneins substitute for copper-zinc superoxide dismutase in vivo to protect cells from oxygen toxicity. Consistent with these results, we show that yeast metallothionein mRNA levels are dramatically elevated under conditions of oxidative stress. Furthermore, in vitro assays demonstrate that yeast metallothionein, purified or from whole-cell extracts, exhibits copper-dependent antioxidant activity. Taken together, these data suggest that both yeast and mammalian metallothioneins may play a direct role in the cellular defense against oxidative stress by functioning as antioxidants.

Animals↗
PubMed1998

Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins.

The nature of chaperone action in the eukaryotic cytosol that assists newly translated cytosolic proteins to reach the native state has remained poorly defined. Actin, tubulin, and Galpha transducin are assisted by the cytosolic chaperonin, CCT, but many other proteins, for example, ornithine transcarbamoylase (OTC), a cytosolic homotrimeric enzyme of yeast, do not require CCT action. Here, we observe that yeast cytosolic OTC is assisted to its native state by the SSA class of yeast cytosolic Hsp70 proteins. In vitro, refolding of OTC diluted from denaturant was assisted by crude yeast cytosol and ATP and found to be directed by SSA1/2. In vivo, when OTC was induced in a temperature-sensitive SSA-deficient strain, it exhibited reduced specific activity, and nonnative subunits were detected in the soluble fraction. These findings indicate that, in vivo, the Hsp70 system assists in folding at least some newly translated cytosolic enzymes, most likely functioning in a posttranslational manner.

Adenosine Triphosphate↗
PubMed2003

Zinc finger protein Prz1 regulates Ca2+ but not Cl- homeostasis in fission yeast. Identification of distinct branches of calcineurin signaling pathway in fission yeast.

Calcineurin is an important mediator that connects the Ca(2+)-dependent signaling to various cellular responses in a wide variety of cell types and organisms. In budding yeast, activated calcineurin exerts its function mainly by regulating the Crz1p/Tcn1 transcription factor. Here, we cloned the fission yeast prz1(+) gene, which encodes a zinc finger transcription factor highly homologous to Crz1/Tcn1. Similar to the results in budding yeast, calcineurin dephosphorylated Prz1 and resulted in the trans-location of Prz1 from the cytoplasm to the nucleus. Prz1 expression was stimulated by high extracellular Ca(2+) in a calcineurin-dependent fashion. However, unlike in budding yeast, the prz1-null cells did not show any phenotype similar to those previously reported in calcineurin deletion such as aberrant cell morphology, mating defect, or hypersensitivity to Cl(-). Instead, the prz1-null cells showed hypersensitivity to Ca(2+), consistent with a dramatic decrease in transcription of Pmc1 Ca(2+) pump. Interestingly, overexpression of Prz1 did not suppress the Cl(-) hypersensitivity of calcineurin deletion, and overexpression of Pmp1 MAPK phosphatase suppressed the Cl(-) hypersensitivity of calcineurin deletion but not the Ca(2+) hypersensitivity of prz1 deletion. In addition, mutations in the its2(+)/cps1(+), its8(+), and its10(+)/cdc7(+) genes that showed synthetic lethal genetic interaction with calcineurin deletion did not exhibit synthetic lethality with the prz1 deletion. Our results suggest that calcineurin activates at least two distinct signaling branches, i.e. the Prz1-dependent transcriptional regulation and an unknown mechanism, which functions antagonistically with the Pmk1 MAPK pathway.

Amino Acid Sequence↗