The effects of 5'-capping, 3'-polyadenylation and leader composition upon the translation and stability of mRNA in a cell-free extract derived from the yeast Saccharomyces cerevisiae

1992 ◽  
Vol 6 (16) ◽  
pp. 2339-2348 ◽  
Author(s):  
Birgit Gerstel ◽  
Mick F. Tuite ◽  
John E. G. McCarthy
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Free Extract ◽  
Yeast Saccharomyces Cerevisiae ◽  
A Cell

Cellular Differentiation in Response to Nutrient Availability: The Repressor of Meiosis, Rme1p, Positively Regulates Invasive Growth in Saccharomyces cerevisiae

Genetics ◽  
2003 ◽  
Vol 165 (3) ◽  
pp. 1045-1058
Author(s):  
Dewald van Dyk ◽  
Guy Hansson ◽  
Isak S Pretorius ◽  
Florian F Bauer
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cellular Differentiation ◽  
Promoter Sequence ◽  
Quiescent State ◽  
Invasive Growth ◽  
Limited Growth ◽  
Yeast Saccharomyces Cerevisiae ◽  
A Cell ◽  
Signaling Modules ◽  
Differentiation Pathways

Abstract In the yeast Saccharomyces cerevisiae, the transition from a nutrient-rich to a nutrient-limited growth medium typically leads to the implementation of a cellular adaptation program that results in invasive growth and/or the formation of pseudohyphae. Complete depletion of essential nutrients, on the other hand, leads either to entry into a nonbudding, metabolically quiescent state referred to as G0 in haploid strains or to meiosis and sporulation in diploids. Entry into meiosis is repressed by the transcriptional regulator Rme1p, a zinc-finger-containing DNA-binding protein. In this article, we show that Rme1p positively regulates invasive growth and starch metabolism in both haploid and diploid strains by directly modifying the transcription of the FLO11 (also known as MUC1) and STA2 genes, which encode a cell wall-associated protein essential for invasive growth and a starch-degrading glucoamylase, respectively. Genetic evidence suggests that Rme1p functions independently of identified signaling modules that regulate invasive growth and of other transcription factors that regulate FLO11 and that the activation of FLO11 is dependent on the presence of a promoter sequence that shows significant homology to identified Rme1p response elements (RREs). The data suggest that Rme1p functions as a central switch between different cellular differentiation pathways.

Evidence for cellular control in the synthesis of acetoin or α-ketoisovaleric acid by microorganisms

1974 ◽  
Vol 20 (6) ◽  
pp. 805-811 ◽  
Author(s):  
E. B. Collins ◽  
R. A. Speckman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Steady State ◽  
Serratia Marcescens ◽  
Lactobacillus Casei ◽  
Optically Active ◽  
Cell Free Extract ◽  
Data Support ◽  
A Cell ◽  
Cellular Control ◽  
Spent Media

Commercial α-acetolactate at pH 4.5 decarboxylated nonenzymatically (5 to 8%/h) to acetoin (69%) and diacetyl (31%), and an extract of Streptococcus diacetilactis 18-16 produced α-acetolactate (in addition to acetoin and diacetyl) from pyruvate in the presence of TPP and MgSO4. Nevertheless, α-acetolactate was not dispersed into media by any of four microorganisms (S. diacetilactis, strains 18-16 and DRC1, Saccharomyces cerevisiae 299, and Lactobacillus casei 393) that produced diacetyl and acetoin or by one (Serratia marcescens) that produced only acetoin. Lactobacillus casei and S. diacetilactis 18-16 produced unknown compounds that falsely indicated the presence of α-acetolactate when tests were made without separating acetoin and diacetyl from other components of the spent media. The production of acetoin by S. diacetilactis 18-16 was not inhibited by valine, the acetoin produced by this organism was optically active (+101.0°), and a cell-free extract of S. marcescens did not produce diacetyl while producing a large amount of acetoin. Data support the conclusion that the conversion of pyruvate to acetoin by some microorganisms and to α-ketoisovaleric acid by others is enzymatic and under cellular control, resulting in the synthesis of only steady-state amounts of enzymatically bound α-acetolactate in each of the pathways.

scholarly journals Pheromones and pheromone receptors are the primary determinants of mating specificity in the yeast Saccharomyces cerevisiae.

Genetics ◽  
1989 ◽  
Vol 121 (3) ◽  
pp. 463-476 ◽  
Author(s):  
A Bender ◽  
G F Sprague
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Types ◽  
Haploid Cell ◽  
Wild Type ◽  
Cell Type ◽  
Yeast Saccharomyces Cerevisiae ◽  
A Cells ◽  
Alpha Factor ◽  
A Cell ◽  
Specific Proteins

Abstract Saccharomyces cerevisiae has two haploid cell types, a and alpha, each of which produces a unique set of proteins that participate in the mating process. We sought to determine the minimum set of proteins that must be expressed to allow mating and to confer specificity. We show that the capacity to synthesize alpha-factor pheromone and a-factor receptor is sufficient to allow mating by mat alpha 1 mutants, mutants that normally do not express any alpha- or a-specific products. Likewise, the capacity to synthesize a-factor receptor and alpha-factor pheromone is sufficient to allow a ste2 ste6 mutants, which do not produce the normal a cell pheromone and receptor, to mate with wild-type a cells. Thus, the a-factor receptor and alpha-factor pheromone constitute the minimum set of alpha-specific proteins that must be produced to allow mating as an alpha cell. Further evidence that the pheromones and pheromone receptors are important determinants of mating specificity comes from studies with mat alpha 2 mutants, cells that simultaneously express both pheromones and both receptors. We created a series of strains that express different combinations of pheromones and receptors in a mat alpha 2 background. These constructions reveal that mat alpha 2 mutants can be made to mate as either a cells or as alpha cells by causing them to express only the pheromone and receptor set appropriate for a particular cell type. Moreover, these studies show that the inability of mat alpha 2 mutants to respond to either pheromone is a consequence of two phenomena: adaptation to an autocrine response to the pheromones they secrete and interference with response to alpha factor by the a-factor receptor.

scholarly journals Identification of genes required for normal pheromone-induced cell polarization in Saccharomyces cerevisiae.

Genetics ◽  
1994 ◽  
Vol 136 (4) ◽  
pp. 1287-1296 ◽  
Author(s):  
J Chenevert ◽  
N Valtz ◽  
I Herskowitz
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Surface ◽  
Cell Polarity ◽  
Vegetative Growth ◽  
Cell Polarization ◽  
Yeast Saccharomyces Cerevisiae ◽  
A Cell ◽  
Uniform Manner ◽  
Mating Factor ◽  
Type Strains

Abstract In response to mating pheromones, cells of the yeast Saccharomyces cerevisiae adopt a polarized "shmoo" morphology, in which the cytoskeleton and proteins involved in mating are localized to a cell-surface projection. This polarization is presumed to reflect the oriented morphogenesis that occurs between mating partners to facilitate cell and nuclear fusion. To identify genes involved in pheromone-induced cell polarization, we have isolated mutants defective in mating to an enfeebled partner and studied a subset of these mutants. The 34 mutants of interest are proficient for pheromone production, arrest in response to pheromone, mate to wild-type strains, and exhibit normal cell polarity during vegetative growth. The mutants were divided into classes based on their morphological responses to mating pheromone. One class is unable to localize cell-surface growth in response to mating factor and instead enlarges in a uniform manner. These mutants harbor special alleles of genes required for cell polarization during vegetative growth, BEM1 and CDC24. Another class of mutants forms bilobed, peanut-like shapes when treated with pheromone and defines two genes, PEA1 and PEA2. PEA1 is identical to SPA2. A third class forms normally shaped but tiny shmoos and defines the gene TNY1. A final group of mutants exhibits apparently normal shmoo morphology. The nature of their mating defect is yet to be determined. We discuss the possible roles of these gene products in establishing cell polarity during mating.

scholarly journals p34Cdc28-mediated control of Cln3 cyclin degradation.

1995 ◽  
Vol 15 (2) ◽  
pp. 731-741 ◽  
Author(s):  
J Yaglom ◽  
M H Linskens ◽  
S Sadis ◽  
D M Rubin ◽  
B Futcher ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
G1 Phase ◽  
Phosphorylation Sites ◽  
Nonpermissive Temperature ◽  
Yeast Saccharomyces Cerevisiae ◽  
Rapid Degradation ◽  
Ubiquitin Conjugating Enzyme ◽  
A Cell ◽  
Cdc28 Kinase ◽  
Beta Galactosidase

Cln3 cyclin of the budding yeast Saccharomyces cerevisiae is a key regulator of Start, a cell cycle event in G1 phase at which cells become committed to division. The time of Start is sensitive to Cln3 levels, which in turn depend on the balance between synthesis and rapid degradation. Here we report that the breakdown of Cln3 is ubiquitin dependent and involves the ubiquitin-conjugating enzyme Cdc34 (Ubc3). The C-terminal tail of Cln3 functions as a transferable signal for degradation. Sequences important for Cln3 degradation are spread throughout the tail and consist largely of PEST elements, which have been previously suggested to target certain proteins for rapid turnover. The Cln3 tail also appears to contain multiple phosphorylation sites, and both phosphorylation and degradation of Cln3 are deficient in a cdc28ts mutant at the nonpermissive temperature. A point mutation at Ser-468, which lies within a Cdc28 kinase consensus site, causes approximately fivefold stabilization of a Cln3-beta-galactosidase fusion protein that contains a portion of the Cln3 tail and strongly reduces the phosphorylation of this protein. These data indicate that the degradation of Cln3 involves CDC28-dependent phosphorylation events.

scholarly journals The RAD7, RAD16, and RAD23 genes of Saccharomyces cerevisiae: requirement for transcription-independent nucleotide excision repair in vitro and interactions between the gene products.

1997 ◽  
Vol 17 (2) ◽  
pp. 635-643 ◽  
Author(s):  
Z Wang ◽  
S Wei ◽  
S H Reed ◽  
X Wu ◽  
J Q Svejstrup ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Nucleotide Excision Repair ◽  
Protein Complex ◽  
Excision Repair ◽  
Dna Lesions ◽  
Yeast Saccharomyces Cerevisiae ◽  
Free System ◽  
Nucleotide Excision ◽  
A Cell

Nucleotide excision repair (NER) is a biochemical process required for the repair of many different types of DNA lesions. In the yeast Saccharomyces cerevisiae, the RAD7, RAD16, and RAD23 genes have been specifically implicated in NER of certain transcriptionally repressed loci and in the nontranscribed strand of transcriptionally active genes. We have used a cell-free system to study the roles of the Rad7, Rad16, and Rad23 proteins in NER. Transcription-independent NER of a plasmid substrate was defective in rad7, rad16, and rad23 mutant extracts. Complementation studies with a previously purified NER protein complex (nucleotide excision repairosome) indicate that Rad23 is a component of the repairosome, whereas Rad7 and Rad16 proteins were not found in this complex. Complementation studies with rad4, rad7, rad16, and rad23 mutant extracts suggest physical interactions among these proteins. This conclusion was confirmed by experiments using the yeast two-hybrid assay, which demonstrated the following pairwise interactions: Rad4 with Rad23, Rad4 with Rad7, and Rad7 with Rad16. Additionally, interaction between the Rad7 and Rad16 proteins was demonstrated in vitro. Our results show that Rad7, Rad16, and Rad23 are required for transcription-independent NER in vitro. This process may involve a unique protein complex which is distinct from the repairosome and which contains at least the Rad4, Rad7, and Rad16 proteins.

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