Identification and phylogenetic classification of eleven putative P-type calcium transport ATPase genes in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe

1996 ◽  
Vol 16 (2) ◽  
pp. 75-85 ◽  
Author(s):  
P. Catty ◽  
A. Goffeau

Calcium is an essential second messenger in yeast metabolism and physiology. So far, only four genes coding for calcium translocating ATPases had been discovered in yeast. The recent completion of the yeast Saccharomyces cerevisiae genome allowed us to identify six new putative Ca++-ATPases encoding genes. Protein sequence homology analysis and phylogenetic classification of all putative Ca++-ATPase gene products from the yeasts Saccharomyces cerevisiae and Schizosacchraomyces pombe reveal three clusters of homologous proteins. Two of them comprises seven proteins which might belong to a new class of P-type ATPases of unknown subcellular location and of unknown physiological function.

FEBS Letters ◽  
1997 ◽  
Vol 409 (3) ◽  
pp. 325-332 ◽  
Author(s):  
Patrice Catty ◽  
Alban de Kerchove d'Exaerde ◽  
André Goffeau

2006 ◽  
Vol 5 (2) ◽  
pp. 330-346 ◽  
Author(s):  
Scott A. Chasse ◽  
Paul Flanary ◽  
Stephen C. Parnell ◽  
Nan Hao ◽  
Jiyoung Y. Cha ◽  
...  

ABSTRACT A common property of G protein-coupled receptors is that they become less responsive with prolonged stimulation. Regulators of G protein signaling (RGS proteins) are well known to accelerate G protein GTPase activity and do so by stabilizing the transition state conformation of the G protein α subunit. In the yeast Saccharomyces cerevisiae there are four RGS-homologous proteins (Sst2, Rgs2, Rax1, and Mdm1) and two Gα proteins (Gpa1 and Gpa2). We show that Sst2 is the only RGS protein that binds selectively to the transition state conformation of Gpa1. The other RGS proteins also bind Gpa1 and modulate pheromone signaling, but to a lesser extent and in a manner clearly distinct from Sst2. To identify other candidate pathway regulators, we compared pheromone responses in 4,349 gene deletion mutants representing nearly all nonessential genes in yeast. A number of mutants produced an increase (sst2, bar1, asc1, and ygl024w) or decrease (cla4) in pheromone sensitivity or resulted in pheromone-independent signaling (sst2, pbs2, gas1, and ygl024w). These findings suggest that Sst2 is the principal regulator of Gpa1-mediated signaling in vivo but that other proteins also contribute in distinct ways to pathway regulation.


Author(s):  
ISABELLE SYLVAIN ◽  
RACHIDA BENHADDOU ◽  
VINCENT CARRE ◽  
SYLVAIN COTTAZ ◽  
HUGUES DRIGUEZ ◽  
...  

A new class of porphyrins bearing thioglycosyl groups is presented in order to improve targeting of malignant cells and resistance to glycosidases. These compounds were synthesized in four steps. They produced 1 O 2 and their photocytotoxicity against the yeast Saccharomyces cerevisiae was compared with the effect of haematoporphyrin.


1995 ◽  
Vol 15 (4) ◽  
pp. 1999-2009 ◽  
Author(s):  
J N Hirschhorn ◽  
A L Bortvin ◽  
S L Ricupero-Hovasse ◽  
F Winston

Nucleosomes have been shown to repress transcription both in vitro and in vivo. However, the mechanisms by which this repression is overcome are only beginning to be understood. Recent evidence suggests that in the yeast Saccharomyces cerevisiae, many transcriptional activators require the SNF/SWI complex to overcome chromatin-mediated repression. We have identified a new class of mutations in the histone H2A-encoding gene HTA1 that causes transcriptional defects at the SNF/SWI-dependent gene SUC2. Some of the mutations are semidominant, and most of the predicted amino acid changes are in or near the N- and C-terminal regions of histone H2A. A deletion that removes the N-terminal tail of histone H2A also caused a decrease in SUC2 transcription. Strains carrying these histone mutations also exhibited defects in activation by LexA-GAL4, a SNF/SWI-dependent activator. However, these H2A mutants are phenotypically distinct from snf/swi mutants. First, not all SNF/SWI-dependent genes showed transcriptional defects in these histone mutants. Second, a suppressor of snf/swi mutations, spt6, did not suppress these histone mutations. Finally, unlike in snf/swi mutants, chromatin structure at the SUC2 promoter in these H2A mutants was in an active conformation. Thus, these H2A mutations seem to interfere with a transcription activation function downstream or independent of the SNF/SWI activity. Therefore, they may identify an additional step that is required to overcome repression by chromatin.


2021 ◽  
Vol 7 (9) ◽  
pp. 712
Author(s):  
Ticiana Fernandes ◽  
Flávia Silva-Sousa ◽  
Fábio Pereira ◽  
Teresa Rito ◽  
Pedro Soares ◽  
...  

Torulaspora delbrueckii has attracted interest in recent years, especially due to its biotechnological potential, arising from its flavor- and aroma-enhancing properties when used in wine, beer or bread dough fermentation, as well as from its remarkable resistance to osmotic and freezing stresses. In the present review, genomic, biochemical, and phenotypic features of T. delbrueckii are described, comparing them with other species, particularly with the biotechnologically well-established yeast, Saccharomyces cerevisiae. We conclude about the aspects that make this yeast a promising biotechnological model to be exploited in a wide range of industries, particularly in wine and bakery. A phylogenetic analysis was also performed, using the core proteome of T. delbrueckii, to compare the number of homologous proteins relative to the most closely related species, understanding the phylogenetic placement of this species with robust support. Lastly, the genetic tools available for T. delbrueckii improvement are discussed, focusing on adaptive laboratorial evolution and its potential.


Genetics ◽  
2000 ◽  
Vol 155 (4) ◽  
pp. 1593-1606 ◽  
Author(s):  
Mylynda B Schlesinger ◽  
Tim Formosa

Abstract Spt16 and Pob3 form stable heterodimers in Saccharomyces cerevisiae, and homologous proteins have also been purified as complexes from diverse eukaryotes. This conserved factor has been implicated in both transcription and replication and may affect both by altering the characteristics of chromatin. Here we describe the isolation and properties of a set of pob3 mutants and confirm that they have defects in both replication and transcription. Mutation of POB3 caused the Spt− phenotype, spt16 and pob3 alleles displayed severe synthetic defects, and elevated levels of Pob3 suppressed some spt16 phenotypes. These results are consistent with previous reports that Spt16 and Pob3 act in a complex that modulates transcription. Additional genetic interactions were observed between pob3 mutations and the genes encoding several DNA replication factors, including POL1, CTF4, DNA2, and CHL12. pob3 alleles caused sensitivity to the ribonucleotide reductase inhibitor hydroxyurea, indicating a defect in a process requiring rapid dNTP synthesis. Mutation of the S phase checkpoint gene MEC1 caused pob3 mutants to lose viability rapidly under restrictive conditions, revealing defects in a process monitored by Mec1. Direct examination of DNA contents by flow cytometry showed that S phase onset and progression were delayed when POB3 was mutated. We conclude that Pob3 is required for normal replication as well as for transcription.


2002 ◽  
Vol 2 (4-5) ◽  
pp. 154-170 ◽  
Author(s):  
Benoît De Hertogh ◽  
Elvira Carvajal ◽  
Emmanuel Talla ◽  
Bernard Dujon ◽  
Philippe Baret ◽  
...  

2013 ◽  
Vol 454 (3) ◽  
pp. 525-532 ◽  
Author(s):  
Rito Herrera ◽  
María C. Álvarez ◽  
Samuel Gelis ◽  
José Ramos

Living cells accumulate potassium (K+) to fulfil multiple functions. It is well documented that the model yeast Saccharomyces cerevisiae grows at very different concentrations of external alkali cations and keeps high and low intracellular concentrations of K+ and sodium (Na+) respectively. However less attention has been paid to the study of the intracellular distribution of these cations. The most widely used experimental approach, plasma membrane permeabilization, produces incomplete results, since it usually considers only cytoplasm and vacuoles as compartments where the cations are present in significant amounts. By isolating and analysing the main yeast organelles, we have determined the subcellular location of K+ and Na+ in S. cerevisiae. We show that while vacuoles accumulate most of the intracellular K+ and Na+, the cytosol contains relatively low amounts, which is especially relevant in the case of Na+. However K+ concentrations in the cytosol are kept rather constant during the K+-starvation process and we conclude that, for that purpose, vacuolar K+ has to be rapidly mobilized. We also show that this intracellular distribution is altered in four different mutants with impaired vacuolar physiology. Finally, we show that both in wild-type and vacuolar mutants, nuclei contain and keep a relatively constant and important percentage of total intracellular K+ and Na+, which most probably is involved in the neutralization of negative charges.


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