Binding of α-factor pheromone to yeast a cells: Chemical and genetic evidence for an α-factor receptor

Jenness, Duane D.; Burkholder, Anne; Hartwell, Leland H.

doi:10.1016/0092-8674(83)90186-1

Cited by 216 publications

(149 citation statements)

References 22 publications

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“…We then tested the possibility that other a-specific genes could also be expressed by performing semi-quantitative RT-PCR analysis, using as template RNA isolated from wild-type and itc1 strains of both mating types. Among the a-specific genes, we analysed STE2, the gene encoding the pheromone a-factor receptor (Blumer et al, 1988;Jenness et al, 1983); BAR1, encoding the protease that degrades a-factor (barrier protease) (Mackay et al, 1988); and ASG7, which has been recently shown to be involved in the regulation of the zygotic transition to vegetative growth (Roth et al, 2000). As shown in Fig.…”

Section: A-specific Genes Are Derepressed In the Mata Itc1 Mutantmentioning

confidence: 99%

Cell-type-dependent repression of yeast a-specific genes requires Itc1p, a subunit of the Isw2p–Itc1p chromatin remodelling complex

et al. 2003

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In Saccharomyces cerevisiae MATa haploid cells, the a-specific genes are expressed, whereas in the MATa haploid and MATa/a diploid cell types their transcription is repressed. It is shown in this report that Itc1p, a component of the ATP-dependent Isw2p-Itc1p chromatin remodelling complex, is required for the repression of a-specific genes. It has previously been reported that disruption of the ITC1 gene leads, in MATa cells, to an aberrant cell morphology resembling the polarized mating projection of cells responding to pheromone. The activation of the pheromone signalling pathway in itc1 mutants of both mating types was examined and found to be constitutively active in MATa itc1 but not in MATa itc1 cells. Furthermore, unlike the wild-type, MATa itc1 and MATa/a itc1/itc1 cells secrete a-factor and express significant levels of other a-specific genes. The results indicate that the inappropriate a-factor production in a MATa context, due to the derepression of the a-specific genes, produces an autocrine signalling loop that leads to the aberrant morphology displayed by MATa itc1 cells. It is suggested that the Isw2p-Itc1p complex contributes to maintain the repressive chromatin structure described for the asg operator present in the promoters of a-specific genes.

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Section: A-specific Genes Are Derepressed In the Mata Itc1 Mutantmentioning

confidence: 99%

Cell-type-dependent repression of yeast a-specific genes requires Itc1p, a subunit of the Isw2p–Itc1p chromatin remodelling complex

et al. 2003

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“…Are important molecules internalized from the growth medium, or would endocytosis just serve to balance the plasma membrane area? The a-factor is a yeast pheromone, which binds apparently to specific receptors on the surface of opposite mating type cells, leading to the early stages of conjugation (see Thorner, 1982;Jenness et al, 1983). …”

Section: Introductionmentioning

confidence: 99%

Endocytosis in Saccharomyces cerevisiae: internalization of alpha-amylase and fluorescent dextran into cells.

Makarow¹

1985

The EMBO Journal

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'The author has published her earlier work under the name Marja Pesonen. Communicated by L.KaariainenIn the preceding paper I reported that Saccharomyces cerevisiae spheroplasts were able to internalize particulate markers, enveloped viruses, into intracellular organelles. Here the internaliation of soluble macromolecules into cells having an intact cell wall is described. a-Amylase was taken up into cells in a temperature-and concentration-dependent way. The kinetics of accumulation were linear for the firt 20-40 min at 37°C and then started to level off. Internalization of aamylase into spheroplasts displayed similar characteristics, but the accumulation rate was about four times higher than into cells. Fluorescent dextran was used to mark morphologically the compartment into which internalization occurred. This marker was accumulated into the vacuole of the cells in a time-, temperature-and concentration-dependent way. A temperature-sensitive mutant deficient in exocytosis was found to be defective in intracellular accumulation of aamylase and dextran. At the restrictive temperature, very little a-amylase accumulated into the cells and only faint staining of intracellular organelles with fluorescent dextran could be detected. At the permissive temperatures, accumulation of a-amylase and dextran into the mutant cells was comparable with accumulation into wild-type cells. I conclude that a-amylase and fluorescent dextran were internalized into S. cerevisiae cells and directed into the vacuoles.

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“…4). 8,59 The straight line of the Scatchard plot indicates that the interaction of detector Halo assay as measured by the growth arrest. For each peptide (6 × 10 −3 M), 0.01 μL (0.1 μg)-10 μL (100 μg) were spotted on discs which were placed upon YEPD plates containing S. cerevisiae 7925 (1.2 × 10 6 cells).…”

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confidence: 99%

Highly Active Analogs of α-Factor and Their Activities Against Saccharomyces cerevisiae

Ahn¹,

Hong²,

Jin³

et al. 2014

Bulletin of the Korean Chemical Society

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Thirteen analogs of tridecapeptide α-factor (WHWLQLKPGQPMY) of Saccharomyces cerevisiae with C-or N-terminal Trp extension and isosteric replacement by Aib at position 8 and 11, Trp at position 13, D-Ala at position 9, and Orn and Glu at position 6 were synthesized and assayed for their biological activity. Receptor binding assay was carried out using our newly developed spectrophotometric method with detector peptide 14. C-or N-terminal extended analogs, α-factor-[Trp] n (n =1-5) 1-5 and [N-Trp] 1 -α-factor 6, were all less active than native α-factor and gradual decreases in both activity and receptor affinity were observed with greater Trp extension. Trp-substituted analog at position 13, [Trp 13 ]α-factor 7, exhibited about 2-fold reductions in both activity and receptor affinity. Aib-substituted analogs, [Aib 8 ]α-factor 8 and [Aib 11]α-factor 9, showed 5-to 10-fold reduction in activity as well as 3-fold reduction in receptor affinity compared to native α-factor. [Orn 6]α-factor 10 demonstrated strong potency with a 7.0-fold increase in halo activity as well as 1.8-fold increase in receptor affinity compared to native α-factor. ]α-factor 11 exhibited 15-fold higher halo activity as well as nearly 3-fold higher receptor affinity compared to native α-factor.

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Binding of α-factor pheromone to yeast a cells: Chemical and genetic evidence for an α-factor receptor

Cited by 216 publications

References 22 publications

Cell-type-dependent repression of yeast a-specific genes requires Itc1p, a subunit of the Isw2p–Itc1p chromatin remodelling complex

Cell-type-dependent repression of yeast a-specific genes requires Itc1p, a subunit of the Isw2p–Itc1p chromatin remodelling complex

Endocytosis in Saccharomyces cerevisiae: internalization of alpha-amylase and fluorescent dextran into cells.

Highly Active Analogs of α-Factor and Their Activities Against Saccharomyces cerevisiae

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