Heterologous expression and characterization of Schizosaccharomyces pombe vacuolar carboxypeptidase Y in Saccharomyces cerevisiae

2002 ◽  
Vol 42 (5) ◽  
pp. 252-259 ◽  
Author(s):  
Kaoru Takegawa ◽  
Sanae Tokudomi ◽  
M. Shah Alam Bhuiyan ◽  
Mitsuaki Tabuchi ◽  
Yasuko Fujita ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Heterologous Expression ◽  
Schizosaccharomyces Pombe ◽  
Carboxypeptidase Y

scholarly journals Heterologous expression and characterization of bacterial 2-C-methyl-d-erythritol-4-phosphate pathway in Saccharomyces cerevisiae

2013 ◽  
Vol 97 (13) ◽  
pp. 5753-5769 ◽  
Author(s):  
Simon Carlsen ◽  
Parayil Kumaran Ajikumar ◽  
Luca Riccardo Formenti ◽  
Kang Zhou ◽  
Too Heng Phon ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Heterologous Expression

Partial characterization of an RNA component that copurifies with Saccharomyces cerevisiae RNase P

1989 ◽  
Vol 9 (6) ◽  
pp. 2536-2543
Author(s):  
J Y Lee ◽  
D R Engelke
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Secondary Structure ◽  
Schizosaccharomyces Pombe ◽  
Rnase P ◽  
Partial Characterization ◽  
Rna Sequences ◽  
Extensive Sequence ◽  
Sequence Similarities

Saccharomyces cerevisiae cellular RNase P is composed of both protein and RNA components that are essential for activity. The isolated holoenzyme contains a highly structured RNA of 369 nucleotides that has extensive sequence similarities to the 286-nucleotide RNA associated with Schizosaccharomyces pombe RNase P but bears little resemblance to the analogous RNA sequences in procaryotes or S. cerevisiae mitochondria. Even so, the predicted secondary structure of S. cerevisiae RNA is strikingly similar to the bacterial phylogenetic consensus rather than to previously predicted structures of other eucaryotic RNase P RNAs.

scholarly journals Characterization of Schizosaccharomyces pombe Malate Permease by Expression in Saccharomyces cerevisiae

2001 ◽  
Vol 67 (9) ◽  
pp. 4144-4151 ◽  
Author(s):  
Carole Camarasa ◽  
Frédérique Bidard ◽  
Muriel Bony ◽  
Pierre Barre ◽  
Sylvie Dequin
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Schizosaccharomyces Pombe ◽  
Malic Acid ◽  
Dicarboxylic Acids ◽  
Acid Uptake ◽  
Acid Transport ◽  
Gene Encoding ◽  
Simple Diffusion ◽  
External Ph

ABSTRACT In Saccharomyces cerevisiae, l-malic acid transport is not carrier mediated and is limited to slow, simple diffusion of the undissociated acid. Expression in S. cerevisiae of the MAE1 gene, encodingSchizosaccharomyces pombe malate permease, markedly increased l-malic acid uptake in this yeast. In this strain, at pH 3.5 (encountered in industrial processes),l-malic acid uptake involves Mae1p-mediated transport of the monoanionic form of the acid (apparent kinetic parameters:V max = 8.7 nmol/mg/min;Km = 1.6 mM) and some simple diffusion of the undissociated l-malic acid (Kd = 0.057 min−1). As total l-malic acid transport involved only low levels of diffusion, the Mae1p permease was further characterized in the recombinant strain. l-Malic acid transport was reversible and accumulative and depended on both the transmembrane gradient of the monoanionic acid form and the ΔpH component of the proton motive force. Dicarboxylic acids with stearic occupation closely related to l-malic acid, such as maleic, oxaloacetic, malonic, succinic and fumaric acids, inhibitedl-malic acid uptake, suggesting that these compounds use the same carrier. We found that increasing external pH directly inhibited malate uptake, resulting in a lower initial rate of uptake and a lower level of substrate accumulation. In S. pombe, proton movements, as shown by internal acidification, accompanied malate uptake, consistent with the proton/dicarboxylate mechanism previously proposed. Surprisingly, no proton fluxes were observed during Mae1p-mediated l-malic acid import inS. cerevisiae, and intracellular pH remained constant. This suggests that, in S. cerevisiae, either there is a proton counterflow or the Mae1p permease functions differently from a proton/dicarboxylate symport.

scholarly journals Functional Expression and Characterization of Schizosaccharomyces pombe Avt3p as a Vacuolar Amino Acid Exporter in Saccharomyces cerevisiae

PLoS ONE ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. e0130542 ◽  
Author(s):  
Soracom Chardwiriyapreecha ◽  
Kunio Manabe ◽  
Tomoko Iwaki ◽  
Miyuki Kawano-Kawada ◽  
Takayuki Sekito ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Schizosaccharomyces Pombe ◽  
Functional Expression

scholarly journals Partial characterization of an RNA component that copurifies with Saccharomyces cerevisiae RNase P.

1989 ◽  
Vol 9 (6) ◽  
pp. 2536-2543 ◽  
Author(s):  
J Y Lee ◽  
D R Engelke
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Secondary Structure ◽  
Schizosaccharomyces Pombe ◽  
Rnase P ◽  
Partial Characterization ◽  
Rna Sequences ◽  
Extensive Sequence ◽  
Sequence Similarities

Saccharomyces cerevisiae cellular RNase P is composed of both protein and RNA components that are essential for activity. The isolated holoenzyme contains a highly structured RNA of 369 nucleotides that has extensive sequence similarities to the 286-nucleotide RNA associated with Schizosaccharomyces pombe RNase P but bears little resemblance to the analogous RNA sequences in procaryotes or S. cerevisiae mitochondria. Even so, the predicted secondary structure of S. cerevisiae RNA is strikingly similar to the bacterial phylogenetic consensus rather than to previously predicted structures of other eucaryotic RNase P RNAs.

scholarly journals Purification and characterization of the invertase from Schizosaccharomyces pombe. A comparative analysis with the invertase from Saccharomyces cerevisiae

1990 ◽  
Vol 267 (3) ◽  
pp. 697-702 ◽  
Author(s):  
S Moreno ◽  
Y Sanchez ◽  
L Rodriguez
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Schizosaccharomyces Pombe ◽  
Molecular Mass ◽  
Total Mass ◽  
High Molecular Mass ◽  
Carbohydrate Moiety ◽  
Purification And Characterization ◽  
Protein Moiety ◽  
Protein Portion

Invertase (EC 3.2.1.26) was purified to homogeneity from exponentially growing cells of Schizosaccharomyces pombe fully de-repressed for synthesis of the enzyme, and was shown to be a high-molecular-mass glycoprotein that can be dissociated in the presence of 8 M-urea/1% SDS into identical subunits with an apparent molecular mass of 205 kDa. The carbohydrate moiety, accounting for 67% of the total mass, is composed of equimolar amounts of mannose and galactose. There is a small amount of glucosamine, which is probably involved in the linkage to the protein moiety, since the enzyme is sensitive to treatment with endoglycosidase H. The composition of the carbohydrate moiety resembles that found in higher-eukaryotic glycoproteins and differs from glycoproteins found in Saccharomyces cerevisiae. The protein portion of each subunit is a polypeptide of molecular mass 60 kDa, very similar to the invertase of Sacch. cerevisiae. Both proteins cross-react with antibodies raised against the protein fractions of the other, indicating that the two enzymes are similar.

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