Saccharomyces cerevisiae a- and alpha-agglutinin: characterization of their molecular interaction.

Cappellaro, Corinna; Hauser, Karin; Mrša, Vladimir; Watzele, Manfred; Watzele, G; Gruber, Clemens; Tanner, Widmar

doi:10.1002/j.1460-2075.1991.tb04984.x

Cited by 100 publications

(77 citation statements)

References 46 publications

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“…This is the case for PIR3, PST1, SED1, YGP1, and SPI1, also known to be induced under poor nutritional conditions (54,(73)(74)(75). Another very important subset of up-regulated genes are those encoding putative ␤-glucanosyl/glucosyltransferase activity (BGL2, CRH1, and SCW10 (76,77)) and ␤-1,3-glucanase (EXG1 (78)). This finding is in accordance with biochemical data showing that cell wall damage provokes an increase in the cross-linking between cell wall polymers and in particular between chitin and ␤-1,6-glucan (reviewed in Ref.…”

Section: Global Expression Changes In Cell Wall Mutants Usingmentioning

confidence: 95%

Genome-wide Analysis of the Response to Cell Wall Mutations in the Yeast Saccharomyces cerevisiae

Lagorce

Hauser

Labourdette

et al. 2003

Journal of Biological Chemistry

241

280

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Perturbations of the yeast cell wall trigger a repair mechanism that reconfigures its molecular structure to preserve cell integrity. To investigate this mechanism, we compared the global gene expression in five mutant strains, each bearing a mutation (i.e. fks1, kre6, mnn9, gas1, and knr4 mutants) that affects in a different manner the cell wall construction. Altogether, 300 responsive genes were kept based on high stringency criteria during data processing. Functional classification of these differentially expressed genes showed a substantial subset of induced genes involved in cell wall construction and an enrichment of metabolic, energy generation, and cell defense categories, whereas families of genes belonging to transcription, protein synthesis, and cellular growth were underrepresented. Clustering methods isolated a single group of ϳ80 up-regulated genes that could be considered as the stereotypical transcriptional response of the cell wall compensatory mechanism. The in silico analysis of the DNA upstream region of these co-regulated genes revealed pairwise combinations of DNA-binding sites for transcriptional factors implicated in stress and heat shock responses (Msn2/4p and Hsf1p) with Rlm1p and Swi4p, two PKC1-regulated transcription factors involved in the activation genes related to cell wall biogenesis and G 1 /S transition. Moreover, this computational analysis also uncovered the 6-bp 5 -AGCCTC-3 CDRE (calcineurindependent response element) motif in 40% of the coregulated genes. This motif was recently shown to be the DNA binding site for Crz1p, the major effector of calcineurin-regulated gene expression in yeast. Taken altogether, the data presented here lead to the conclusion that the cell wall compensatory mechanism, as triggered by cell wall mutations, integrates three major regulatory systems: namely the PKC1-SLT2 mitogen-activated protein kinase-signaling module, the "global stress" response mediated by Msn2/4p, and the Ca 2؉ /calcineurindependent pathway. The relative importance of these regulatory systems in the cell wall compensatory mechanism is discussed.Yeast and fungi are surrounded by a cell wall that is a complex structure essential for maintenance of the cell shape, prevention of lysis, and protection against harmful environmental conditions. The yeast cell wall architecture has been determined in detail over the past decade (1). It is a layered structure that is composed of ␤-1,3-and ␤-1,6-glucan (50 -60% of the cell wall dry mass), mannoproteins (40 -50%), and chitin (2%). ␤-1,3-Glucan and chitin form a fibrillar network to which mannoproteins are anchored, mostly through ␤-1,6-glucan. Some cell wall proteins, like the PIR family, can be directly linked to ␤-1,3-glucan (reviewed in Ref.2). The cell wall is not a rigid structure, since it endures all of the changes that the cell undergoes during division, morphogenesis, and differentiation.To ensure continuous integrity of the wall in accordance with its plasticity, complex mechanisms must be operating, which need to be strictly ...

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Section: Global Expression Changes In Cell Wall Mutants Usingmentioning

confidence: 95%

Genome-wide Analysis of the Response to Cell Wall Mutations in the Yeast Saccharomyces cerevisiae

Lagorce

Hauser

Labourdette

et al. 2003

Journal of Biological Chemistry

241

280

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“…One of these is the MATa-specific a-factor protease, Bar1 (Sprague and Herskowitz 1981;MacKay et al 1988), which helps MATa cells detect an a-factor gradient and polarize toward MATa partners (Jackson and Hartwell 1990; Barkai et al 1998). Yeast cells also express mating-type-specific agglutinins, which help cells attach to mating partners (Cappellaro et al 1991) in liquid but individually have little effect on mating efficiency on solid media (Lipke et al 1989;Roy et al 1991;de Nobel et al 1995). Evidence for the final, characterized MATa-specific gene was produced by Bender and Sprague (1989) who noted that cells expressing MATa-specific proteins and Ste3 were unable to mount a pheromone response.…”

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confidence: 99%

Genetically Engineered Transvestites Reveal Novel Mating Genes in Budding Yeast

Huberman

Murray

2013

Genetics

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Haploid budding yeast has two mating types, defined by the alleles of the MAT locus, MATa and MATa. Two haploid cells of opposite mating types mate by signaling to each other using reciprocal pheromones and receptors, polarizing and growing toward each other, and eventually fusing to form a single diploid cell. The pheromones and receptors are necessary and sufficient to define a mating type, but other mating-type-specific proteins make mating more efficient. We examined the role of these proteins by genetically engineering "transvestite" cells that swap the pheromone, pheromone receptor, and pheromone processing factors of one mating type for another. These cells mate with each other, but their mating is inefficient. By characterizing their mating defects and examining their transcriptomes, we found Afb1 (a-factor barrier), a novel MATa-specific protein that interferes with a-factor, the pheromone secreted by MATa cells. Strong pheromone secretion is essential for efficient mating, and the weak mating of transvestites can be improved by boosting their pheromone production. Synthetic biology can characterize the factors that control efficiency in biological processes. In yeast, selection for increased mating efficiency is likely to have continually boosted pheromone levels and the ability to discriminate between partners who make more and less pheromone. This discrimination comes at a cost: weak mating in situations where all potential partners make less pheromone. BIOLOGICAL processes are typically defined by the genes that are necessary and sufficient for function. However, in many cases, this minimal gene set does not encompass all the proteins involved in a process, and additional proteins promote biological efficiency. Finding these additional proteins may require the detection of subtle phenotypes, making it hard to know if all the genes involved in a process have been identified. One way to answer this question is to reengineer a pathway and ask whether the synthetic version fully mimics the natural function. Here, we show that this form of synthetic biology illuminates how cells of the budding yeast Saccharomyces cerevisiae mate efficiently.Budding yeast can be stably maintained as haploids or diploids. Haploids mate when two cells of opposite mating types signal to each other using reciprocal pheromones and receptors, polarize and grow toward each other, and eventually fuse to form a single diploid. Yeast has two mating types, a and a ( Figure 1A), determined by two alternative alleles at the MAT locus, MATa and MATa, which encode different transcription factors (Herskowitz 1988). These factors regulate the expression of mating-type-specific genes, many of which are involved with the production and detection of the pheromones that yeast cells use to signal to one another. The pheromones (a-and a-factor) are detected by G-proteincoupled receptors. MATa cells express a-factor (Betz and Duntze 1979), which is secreted through an ATP binding cassette transporter (Ste6) (McGrath and Varshavsky 1989)...

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“…n et al, 1999). In this case, the protein was also retained in the wall by disulfide bridges to lattice proteins, as in S. cerevisiae (Cappellaro et al, 1998).…”

Section: Discussionmentioning

confidence: 99%

Secretion, interaction and assembly of two O-glycosylated cell wall antigens from Candida albicans

et al. 2001

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The mechanisms of incorporation of two antigens have been determined using a monoclonal antibody (3A10) raised against the material released from the mycelial cell wall by zymolyase digestion and retained on a concanavalin A column. One of the hybridomas secreted an IgG that reacted with two bands in Western blots. Indirect immunofluorescence showed that the antigens were located on the surfaces of mycelial cells, but within the cell walls of yeasts. These antigens were detected in a membrane preparation, in the SDS-soluble material and in the material released by a 1,3-β-glucanase and chitinase from the cell walls of yeast and mycelial cells. In the latter three samples, an additional high-molecular-mass, highly polydispersed band was also detected. Beta-elimination of each fraction resulted in the disappearance of all antigen bands, suggesting that they are highly O-glycosylated. In addition, the electrophoretic mobility of the high-molecular-mass, highly polydispersed bands increased after digestion with endoglycosidase H, indicating that they are also N-glycosylated. New antigen bands were released when remnants of the cell walls extracted with 1,3-β-glucanase or chitinase were digested with chitinase or 1,3-β-glucanase. These results are consistent with the notion that, after secretion, parts of the O-glycosylated antigen molecules are transferred to an N-glycosylated protein(s). This molecular complex, as well as the remaining original 70 and 80 kDa antigen molecules, next bind to 1,3-β-glucan or chitin, probably via 1,6-β-glucan, and, in an additional step, to chitin or 1,3-β-glucan. This process results in the final molecular product of each antigen, and their distribution in the cell walls.

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Saccharomyces cerevisiae a- and alpha-agglutinin: characterization of their molecular interaction.

Cited by 100 publications

References 46 publications

Genome-wide Analysis of the Response to Cell Wall Mutations in the Yeast Saccharomyces cerevisiae

Genome-wide Analysis of the Response to Cell Wall Mutations in the Yeast Saccharomyces cerevisiae

Genetically Engineered Transvestites Reveal Novel Mating Genes in Budding Yeast

Secretion, interaction and assembly of two O-glycosylated cell wall antigens from Candida albicans

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