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PubMed1964

RECOMBINATION BETWEEN NOCARDIA ERYTHROPOLIS AND NOCARDIA CANICRURIA.

Adams, James N. (University of South Dakota, Vermillion). Recombination between Nocardia erythropolis and Nocardia canicruria. J. Bacteriol. 88:865-876. 1964.-Nutritionally complementary auxotrophic mutants derived from Nocardia erythropolis did not yield prototrophic recombinants when progeny from mixed cultures or newly mixed strains were inoculated onto minimal medium. Similarly, complementary auxotrophic mutants of N. canicruria did not produce prototrophic recombinants. When interspecific mating was attempted between complementary mutants of N. erythropolis and N. canicruria, prototrophic recombinants were recovered at frequencies dependent, in part, upon the auxotrophic strains used in the test crosses. Growth of the parental types in mixed cultures was necessary for the production of recombinant progeny. Direct selection for recombinants by inoculating the selective medium with a mixture of parental types without prior mixed growth did not result in the recovery of recombinants. Varying the medium upon which mixed growth occurred, or varying the ratio of N. erythropolis to N. canicruria cells used as inocula, did not greatly affect the recovery of recombinants. Heat-killing one or the other of the parental types prevented recombinant production. The lack of recovery of recombinants from crosses of homologously derived strains suggested that a mating factor controls recombination. The mating factor was not eliminated by acriflavine treatment. The recovery of a recombinant strain capable of forming recombinants with either N. erythropolis or N. canicruria, and the recovery of another strain which mated only with N. erythropolis in backcrosses, suggests that the mating factor may be of a multiple nature.

Adenine↗

PubMed1983

Isolation of the mating-inducing factor of the ciliate Euplotes.

Numerous strains of different mating types of the marine ciliate Euplotes raikovi have been found to be autonomous excreters into the surrounding medium of specific mating-inducing factors (gamones) (Luporini, P et al., J exp zool 226 (1983) 1 [9]). The gamone from the mating type represented by strain 13 has been isolated and identified as a glycoprotein with a molecular weight (MW) of about 12 kD and a pI of 4. It has been termed euplomone r 13. At a concentration of 3 X 10(-12) M, euplomone r 13 specifically induces cells of a complementary mating type to unite in conjugation within 2 h.

Animals↗

PubMed2002

Peptide inhibitors of appressorium development in Glomerella cingulata.

The phytopathogen Glomerella cingulata (anamorph: Colletotrichum gloeosporioides) infects host tissue by means of a specialised infection structure, the appressorium. The Saccharomyces cerevisiae alpha-mating factor pheromone, the Saccharomyces kluyveri alpha-mating factor pheromone and a hendecapeptide produced by G. cingulata inhibit appressorium development. The amino acid sequence of the G. cingulata peptide, GYFSYPHGNLF, is different from that of the mature pheromone peptides of other filamentous fungi. The peptide has sequence similarity with the Saccharomyces alpha-mating factor pheromones, but is unable to elicit growth arrest in S. cerevisiae.

Amino Acid Sequence↗

PubMed1992

Characterization of the energy-dependent, mating factor-activated Ca2+ influx in Saccharomyces cerevisiae.

The yeast mating pheromones, a and alpha factors, bind to specific G protein-coupled receptors in haploid cells and bring about both growth arrest in the early G1 phase of the cell cycle and differentiation into mating capable cells. This induces an increase in Ca2+ influx leading to elevated intracellular calcium concentrations, which has been shown to be essential for subsequent downstream events and the mating process itself [1]. We have characterized the alpha factor induced increase in cellular Ca2+ in wild type S. cerevisiae and in the temperature-sensitive cell division cycle mutants cdc7 and cdc28 which are growth-arrested at the G0-G1 border at the nonpermissive temperature. We observed a 2-4 fold increase in the initial velocity of Ca2+ influx in alpha factor-treated wild-type cells and in cdc7 and cdc28 cells grown at the nonpermissive temperature. Calcium influx was energy dependent, inhibited by membrane depolarization and slightly increased by hyperpolarization. Furthermore, Ca2+ influx was sensitive to both divalent and trivalent cations, but was unaffected by nifedipine and verapamil. These data demonstrate that budding yeast possesses a regulated Ca2+ transport mechanism, the activation of which is dependent upon exit out of the cell cycle and growth cessation. This transport mechanism has many similarities to that observed in mitogen-stimulated mammalian cells.

2,4-Dinitrophenol↗

PubMed1979

Purification and partial characterization of a factor, a mating hormone produced by mating-type-a cells from Saccharomyces cerevisiae.

Cells of Saccharomyces cerevisiae exhibiting the a mating type secrete into the culture medium a mating-type-specific hormone activity (a factor), which specifically causes a transient arrest of DNA replication and cell division in cells of the opposite mating type, alpha. Three compounds exhibiting a factor activity have been found in culture filtrates from a cells. The most active compound has been purified more than 10(5)-fold and appears to be homogeneous on the basis of thin-layer chromatography and thin-layer electrophoresis in different systems. We propose that this compound, which exhibits in alpha cells the biological activities that have been attributed to a factor, represents pure a factor. a factor has been characterized as a very hydrophobic undecapeptide with the following amino acid composition: H2N-Tyr (Asx1, Gly1, Ala1, Val1, Ile2, Phe1, Lys1, Trp1, Pro1). Although in their respective target cells the biological effects of a factor and of alpha factor, the corresponding mating hormone of mating-type-alpha cells, are remarkably similar, the primary structures of both hormones appear to be quite different.

Agglutination↗

PubMed1998

Conformational analysis of cyclic analogues of the Saccharomyces cerevisiae alpha-factor pheromone.

Analogues of the alpha-factor mating pheromone (WHWLQLKPGQPMY) from Saccharomyces cerevisiae in which the side chains of residues 7 and 10 were joined by lactam bonds were studied by nmr and molecular modeling. These investigations were carried out to discern the effect of lactam ring size on conformation and to ascertain whether the side chain i to i + 3 cyclized tetramers [H. R. Marepalli et al. (1996) Journal of the American Chemical Society, Vol. 118, pp. 6531-6539] can be considered as conformation-constraining building blocks when introduced into a long peptide chain. Nuclear Overhauser effect constraints, temperature coefficients, and backbone torsional angles were derived from 1H-nmr spectra measured in DMSO-d6. Modeling studies using the above constraints indicate that the lactam regions of the tridecapeptides assume various combinations of type II beta-turns, gamma-turns, and gamma 1-turns, but never type I beta-turns. These investigations provide evidence that the tetrapeptide building blocks retain their preferred conformations in larger molecules and can be used to control the architecture of regions of such peptides.

Amino Acid Sequence↗

PubMed1994

Biophysical studies on fragments of the alpha-factor receptor protein.

The receptor for the alpha-factor mating pheromone of the yeast Saccharomyces cerevisiae consists of 431 amino acid residues and is a member of a family of membrane proteins predicted to have seven transmembrane helices. Fragments of the receptor corresponding to two of the transmembrane helices [residues 246-269 (M6) and 273-302 (M7)], two of the interhelical loops [residues 107-125 (E2) and 191-206 (E3)], and to a portion of the carboxyl terminus [residues 350-372 (CT)] were synthesized using solid-phase methodologies and purified to near homogeneity. CD was used to characterize the secondary structure of these peptides in trifluoroethanol (TFE), in TFE/water mixtures, in sodium dodecyl sulfate (SDS), and in the presence of dimyristoyl phosphatidylcholine (DMPC) liposomes. In TFE, M6 and M7 exhibited CD spectra consistent with highly helical peptides, whereas CT was partially helical. In contrast, E2 and E3 were either disordered or aggregated in this solvent. M6 did not partition well into DMPC vesicles whereas M7 remained helical. Both M6 and M7 assumed helical conformations in 25 mM SDS. The loop peptides and the carboxyl terminus peptide were either in a beta-structure or disordered in the presence of lipid. These findings represent the first biophysical evidence for conformations assumed by specific segments of the STE2 receptor protein.

Amino Acid Sequence↗

PubMed1989

Serial section reconstruction using a computer graphics system: applications to intracellular structures in yeast cells and to the periodontal structure of dogs' teeth.

A computer graphics system for reconstruction from serial section micrographs was applied to intracellular details of a yeast target cell (Saccharomyces cerevisiae cell) induced by the alpha factor mating pheromone and was also applied to a periodontal structure of a dog tooth moved orthodontically. In the former, intracellular organelles and a distribution of vesicles could be clearly observed through the cell membrane using the transparent display method in which the smoothing of the reconstructed outer cell membrane surface by computer processing was applied to the transparent display. In the latter case, by cutting through a reconstructed dog tooth and its periodontal tissues, labiolingual and mesiodistal cut surfaces of the tooth and of adjacent alveolar bone could be observed with fine details (232 sections were used).

Animals↗

PubMed2004

Sorting signals can direct receptor-mediated export of soluble proteins into COPII vesicles.

Soluble secretory proteins are first translocated across endoplasmic reticulum (ER) membranes and folded in a specialized ER luminal environment. Fully folded and assembled secretory cargo are then segregated from ER-resident proteins into COPII-derived vesicles or tubular elements for anterograde transport. Mechanisms of bulk-flow, ER-retention and receptor-mediated export have been suggested to operate during this transport step, although these mechanisms are poorly understood. In yeast, there is evidence to suggest that Erv29p functions as a transmembrane receptor for the export of certain soluble cargo proteins including glycopro-alpha-factor (gpalphaf), the precursor of alpha-factor mating pheromone. Here we identify a hydrophobic signal within the pro-region of gpalphaf that is necessary for efficient packaging into COPII vesicles and for binding to Erv29p. When fused to Kar2p, an ER-resident protein, the pro-region sorting signal was sufficient to direct Erv29p-dependent export of the fusion protein into COPII vesicles. These findings indicate that specific motifs within soluble secretory proteins function in receptor-mediated export from the ER. Moreover, positive sorting signals seem to predominate over potential ER-retention mechanisms that may operate in localizing ER-resident proteins such as Kar2p.

COP-Coated Vesicles↗

PubMed2005

Yeast as a tractable genetic system for functional studies of the insulin-degrading enzyme.

We have developed yeast as an expression and genetic system for functional studies of the insulin-degrading enzyme (IDE), which cleaves and inactivates certain small peptide molecules, including insulin and the neurotoxic A beta peptide. We show that heterologously expressed rat IDE is enzymatically active, as judged by the ability of IDE-containing yeast extracts to cleave insulin in vitro. We also show that IDE can promote the in vivo production of the yeast a-factor mating pheromone, a function normally attributed to the yeast enzymes Axl1p and Ste23p. However, IDE cannot substitute for the function of Axl1p in promoting haploid axial budding and repressing haploid invasive growth, activities that require an uncharacterized activity of Axl1p. Particulate fractions enriched for Axl1p or Ste23p are incapable of cleaving insulin, suggesting that the functional conservation of these enzymes may not be bidirectionally conserved. We have made practical use of our genetic system to confirm that residues composing the extended zinc metalloprotease motif of M16A family enzymes are required for the enzymatic activity of IDE, Ste23p, and Axl1p. We have determined that IDE and Axl1p both require an intact C terminus for optimal activity. We expect that the tractable genetic system that we have developed will be useful for investigating the enzymatic and structure/function properties of IDE and possibly for the identification of novel IDE alleles having altered substrate specificity.

Alleles↗

PubMed1994

Metabolic instability and constitutive endocytosis of STE6, the a-factor transporter of Saccharomyces cerevisiae.

STE6, a member of the ATP binding cassette (ABC) transporter superfamily, is a membrane protein required for the export of the a-factor mating pheromone in Saccharomyces cerevisiae. To initiate a study of the intracellular trafficking of STE6, we have examined its half-life and localization. We report here that STE6 is metabolically unstable in a wild-type strain, and that this instability is blocked in a pep4 mutant, suggesting that degradation of STE6 occurs in the vacuole and is dependent upon vacuolar proteases. In agreement with a model whereby STE6 is routed to the vacuole via endocytosis from the plasma membrane, we show that degradation of STE6 is substantially reduced at nonpermissive temperature in mutants defective in delivery of proteins to the plasma membrane (sec6) or in endocytosis (end3 and end4). Whereas STE6 appears to undergo constitutive internalization from the plasma membrane, as do the pheromone receptors STE2 and STE3, we show that two other proteins, the plasma membrane ATPase (PMA1) and the general amino acid permease (GAP1), are significantly more stable than STE6, indicating that rapid turnover in the vacuole is not a fate common to all plasma membrane proteins in yeast. Investigation of STE6 partial molecules (half- and quarter-molecules) indicates that both halves of STE6 contain sufficient information to mediate internalization. Examination of STE6 localization by indirect immunofluorescence indicates that STE6 is found in a punctate, possibly vesicular, intracellular pattern, distinct from the rim-staining pattern characteristic of PMA1. The punctate pattern is consistent with the view that most of the STE6 molecules present in a cell at any given moment could be en route either to or from the plasma membrane. In a pep4 mutant, STE6 is concentrated in the vacuole, providing further evidence that the vacuole is the site of STE6 degradation, while in an end4 mutant STE6 exhibits rim-staining, indicating that it can accumulate in the plasma membrane when internalization is blocked. Taken together, the results presented here suggest that STE6 first travels to the plasma membrane and subsequently undergoes endocytosis and degradation in the vacuole, with perhaps only a transient residence at the plasma membrane; an alternative model, in which STE6 circumvents the plasma membrane, is also discussed.

ATP-Binding Cassette Transporters↗

PubMed1988

Identification of a DNA segment that is necessary and sufficient for alpha-specific gene control in Saccharomyces cerevisiae: implications for regulation of alpha-specific and a-specific genes.

STE3 mRNA is present only in Saccharomyces cerevisiae alpha cells, not in a or a/alpha cells, and the transcript level increases about fivefold when cells are treated with a-factor mating pheromone. Deletions in the 5' noncoding region of STE3 defined a 43-base-pair (bp) upstream activation sequence (UAS) that can impart both modes of regulation to a CYC1-lacZ fusion when substituted for the native CYC1 UAS. UAS activity required the alpha 1 product of MAT alpha, which is known to be required for transcription of alpha-specific genes. A chromosomal deletion that removed only 14 bp of the STE3 UAS reduced STE3 transcript levels 50- to 100-fold, indicating that the UAS is essential for expression. The STE3 UAS shares a 26-bp homology with the 5' noncoding sequences of the only other known alpha-specific genes, MF alpha 1 and MF alpha 2. We view the homology as having two components--a nearly palindromic 16-bp "P box" and an adjacent 10-bp "Q box." A synthetic STE3 P box was inactive as a UAS; a perfect palindrome P box was active in all three cell types. We propose that the P box is the binding site for a transcription activator, but that alpha 1 acting via the Q box is required for this activator to bind to the imperfect P boxes of alpha-specific genes. Versions of the P box are also found upstream of a-specific genes, within the binding sites of the repressor alpha 2 encoded by MAT alpha. Thus, the products of MAT alpha may render gene expression alpha or a-specific by controlling access of the same transcription activator to its binding site, the P box.

Base Sequence↗

PubMed1994

Production of active, insect-specific scorpion neurotoxin in yeast.

A cDNA encoding the Androctonus australis Hector insect toxin 1 (AaH IT1) was expressed in yeast leading to secretion of fully biologically active protein. Three different multicopy plasmids were constructed using PCR. Expression was directed by the strong PGK1 promoter of the yeast vector pMA 91. Plasmid pMA 91-AaH IT1 encodes AaH IT1 and its own signal peptide. In the two other constructions, the cDNA encoding the mature part of AaH IT1 is fused to the prepro-signal sequence of the yeast alpha-mating-factor precursor; the pBAL 7-alpha-KREAEA-AaH IT1 includes the cDNA sequence encoding the KR(EAEA) processing sequence of the alpha-mating factor, and pBAL 7-alpha-KR-AaH IT1 encodes the KR fused directly to the AaH IT1 gene. The yeast alpha-mating-factor signal peptide launched the pro-alpha-mating-factor-AaH IT1 fusion protein into the secretory pathway. The fusion proteins are expected to be cleaved in the Golgi by the KEX2 endopeptidase and the STE13 dipeptidyl aminopeptidase, leading to release of mature AaH IT1. Pulse/chase labelling of transformed yeast protoplasts, followed by SDS/PAGE analysis of proteins immunoprecipitated from either the lysate or the extracellular fluid, showed that AaH IT1 was produced. The highest concentration of recombinant AaH IT1 in the culture medium, as determined using a 125I-AaH IT1 specific radioimmunoassay, was 4 micrograms/l (0.5 nM). The recombinant toxin was fully biologically active against cockroaches as assessed by injection and comparison to native AaH IT1. Moreover, it competed with radiolabelled native toxin for its receptor on the voltage-sensitive Na+ channel with a dissociation constant of 0.5 nM.

Animals↗

PubMed1999

Expression of MFA1 and STE6 is sufficient for mating type-independent secretion of yeast a-factor, but not mating competence.

The yeast a-factor mating peptide and its transporter Ste6 are normally expressed only in MATa haploid cells. The a-factor is initially produced as a 36- or 38-residue peptide precursor and must undergo extensive post-translational processing to produce an active 12 amino-acid lipopeptide. To better understand the steps required for Ste6-dependent a-factor transport, we have reconstituted a-factor synthesis and transport in MATalpha haploids and MATa/alpha diploids. Ste6 and a-factor were stably expressed in MATalpha and MATa/alpha cells and the ectopically expressed a-factor was correctly processed. In addition, Ste6 was able to transport a-factor from all cell types, indicating that once expressed no other MATa-specific functions are required. However, despite significant levels of a-factor secretion, MATalpha cells are unable to support efficient mating.

ATP-Binding Cassette Transporters↗

PubMed2005

[Influence of B mating-type factor on recovery of nuclear types from dikaryons in Lentinula edodes].

This study determined a genetic basis for the phenomenon of significant asymmetric ratio of the two component nuclear types from dikaryons of Lentinula edodes via protoplast formation and regeneration by clarifying the influence of A or B mating-type factor on recovery of nuclear types from dikuaryons. The results revealed that B factor or some supposed genes linked to the B factor appeared to influence survival of dedikaryotized nuclei,whereas A factor had no apparent effect on this phenomenon. Specificity of B factor was shown to correlate with percentage survival of the component nuclear types recovered from both kinds of heterokaryons (A not equal to B not equal to and A = B not equal to). It can be put in an hierarchical order with respect to this function,the hierarchical order of these B factors was B1 > B3 > B4 > B2 between two tested strains.

Fungal Proteins↗

PubMed1982

Mating-defective ste mutations are suppressed by cell division cycle start mutations in Saccharomyces cerevisiae.

Temperature-sensitive mutants which arrest in the G1 phase of the cell cycle have been described for the yeast Saccharomyces cerevisiae. One class of these mutants (carrying cdc28, cdc36, cdc37, or cdc39) forms a shmoo morphology at restrictive temperature, characteristic of mating pheromone-arrested wild-type cells. Therefore, one hypothesis to explain the control of cell division by mating factors states that mating pheromones arrest wild-type cells by inactivating one or more of these CDC gene products. A class of mutants (carrying ste4, ste5, ste7, ste11, or ste12) which is insensitive to mating pheromone and sterile has also been described. One possible function of the STE gene products is the inactivation of the CDC gene products in the presence of a mating pheromone. A model incorporating these two hypotheses predicts that such STE gene products will not be required for mating in strains carrying an appropriate cdc lesion. This prediction was tested by assaying the mating abilities of double mutants for all of the pairwise combinations of cdc and ste mutations. Lesions in either cdc36 or cdc39 suppressed the mating defect due to ste4 and ste5. Allele specificity was observed in the suppression of both ste4 and ste5. The results indicate that the CDC36, CDC39, STE4, and STE5 gene products interact functionally or physically or both in the regulation of cell division mediated by the presence or absence of mating pheromones. The cdc36 and cdc39 mutations did not suppress ste7, ste11, or ste12. Lesions in cdc28 or cdc37 did not suppress any of the ste mutations. Other models of CDC and STE gene action which predicted that some of the cdc and ste mutations would be alleles of the same locus were tested. None of the cdc mutations was allelic to the ste mutations and, therefore, these models were eliminated.

Cell Division↗

PubMed1998

The role of Cdc42 in signal transduction and mating of the budding yeast Saccharomyces cerevisiae.

The small G-protein Cdc42 functions in many eukaryotic signal transduction pathways. In the budding yeast Saccharomyces cerevisiae, cells with defective Cdc42 fail to induce mating-specific genes in response to mating factor and to adopt the proper morphology for conjugation. Here we show that the failure of mating factor-induced transcription is largely the indirect result of arrest at a specific cell cycle position and/or the accumulation of high levels of the Cln1/2-Cdc28 kinase, a known repressor of mating factor signal transduction. Cdc42-defective cells with restored transcriptional induction have a partially restored mating ability but are still defective in the morphological response to mating factor. These results show that Cdc42 is not required for transduction of the mating factor signal per se but that it is essential for proper mating factor-induced morphogenesis.

CDC28 Protein Kinase, S cerevisiae↗

PubMed1976

Mutants of Saccharomyces cerevisiae resistant to the alpha mating-type factor.

Mutants that are resistant to alpha-factor have been isolated from a mating-type haploid strains of yeast by direct selection on agar medium containing partially purified alpha-factor. All resistant mutants isolated were found to be sterile. They were characterized and compared with mutants previously isolated as non-mating. Among 93 able to mate at low frequency and to sporulate, none showed linkage to the mating-type locus. The results support the hypothesis that the response to alpha-factor by cells of mating-type a is essential for mating.

Cell Differentiation↗