scholarly journals High-Level Secretory Production of Phospholipase A1by Saccharomyces cerevisiae and Aspergillus oryzae

2001 ◽  
Vol 65 (1) ◽  
pp. 94-101 ◽  
Author(s):  
Yoichiro SHIBA ◽  
Chiho ONO ◽  
Fumio FUKUI ◽  
Ichiro WATANABE ◽  
Nobufusa SERIZAWA ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Aspergillus Oryzae ◽  
Secretory Production ◽  
High Level

High-level secretory production of recombinant human lipocortin-I by Saccharomyces cerevisiae

1999 ◽  
Vol 35 (1-2) ◽  
pp. 97-101 ◽  
Author(s):  
Bong Hyun Chung ◽  
Dong Jin Seo ◽  
Soo Wan Nam
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Secretory Production ◽  
High Level

scholarly journals Tempo and Mode of Ty Element Evolution in Saccharomyces cerevisiae

Genetics ◽  
1999 ◽  
Vol 151 (4) ◽  
pp. 1341-1351 ◽  
Author(s):  
I King Jordan ◽  
John F McDonald
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Negative Selection ◽  
Sequence Variation ◽  
Size Variation ◽  
Sequence Comparisons ◽  
Ty Elements ◽  
Ty Element ◽  
Amino Acid Sequence Variation ◽  
Element Evolution ◽  
High Level

Abstract The Saccharomyces cerevisiae genome contains five families of long terminal repeat (LTR) retrotransposons, Ty1–Ty5. The sequencing of the S. cerevisiae genome provides an unprecedented opportunity to examine the patterns of molecular variation existing among the entire genomic complement of Ty retrotransposons. We report the results of an analysis of the nucleotide and amino acid sequence variation within and between the five Ty element families of the S. cerevisiae genome. Our results indicate that individual Ty element families tend to be highly homogenous in both sequence and size variation. Comparisons of within-element 5′ and 3′ LTR sequences indicate that the vast majority of Ty elements have recently transposed. Furthermore, intrafamily Ty sequence comparisons reveal the action of negative selection on Ty element coding sequences. These results taken together suggest that there is a high level of genomic turnover of S. cerevisiae Ty elements, which is presumably in response to selective pressure to escape host-mediated repression and elimination mechanisms.

Functional domains of SIR4, a gene required for position effect regulation in Saccharomyces cerevisiae

1987 ◽  
Vol 7 (12) ◽  
pp. 4441-4452
Author(s):  
M Marshall ◽  
D Mahoney ◽  
A Rose ◽  
J B Hicks ◽  
J R Broach
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Mating Type ◽  
Position Effect ◽  
Protein Activity ◽  
Multicomponent Complex ◽  
Mating Type Genes ◽  
Chromosome Iii ◽  
Covalently Linked ◽  
High Level ◽  
Mat Locus

The product of the Saccharomyces cerevisiae SIR4 gene, in conjunction with at least three other gene products, prevents expression of mating-type genes resident at loci at either end of chromosome III, but not of the same genes resident at the MAT locus in the middle of the chromosome. To address the mechanism of this novel position effect regulation, we have conducted a structural and genetic analysis of the SIR4 gene. We have determined the nucleotide sequence of the gene and found that it encodes a lysine-rich, serine-rich protein of 152 kilodaltons. Expression of the carboxy half of the protein complements a chromosomal nonsense mutation of sir4 but not a complete deletion of the gene. These results suggest that SIR4 protein activity resides in two portions of the molecule, but that these domains need not be covalently linked to execute their biological function. We also found that high-level expression of the carboxy domain of the protein yields dominant derepression of the silent loci. This anti-Sir activity can be reversed by increased expression of the SIR3 gene, whose product is normally also required for maintaining repression of the silent loci. These results are consistent with the hypothesis that SIR3 and SIR4 proteins physically associate to form a multicomponent complex required for repression of the silent mating-type loci.

scholarly journals Transcriptional activation upon pheromone stimulation mediated by a small domain of Saccharomyces cerevisiae Ste12p.

1997 ◽  
Vol 17 (11) ◽  
pp. 6410-6418 ◽  
Author(s):  
H Pi ◽  
C T Chien ◽  
S Fields
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Map Kinase ◽  
Transcriptional Activation ◽  
Transcriptional Activity ◽  
Activation Domain ◽  
Yeast Saccharomyces Cerevisiae ◽  
Activation Domains ◽  
Hybrid Proteins ◽  
High Level ◽  
Transcriptional Induction

In the yeast Saccharomyces cerevisiae, Ste12p induces transcription of pheromone-responsive genes by binding to a DNA sequence designated the pheromone response element. We generated a series of hybrid proteins of Ste12p with the DNA-binding and activation domains of the transcriptional activator Gal4p to define a pheromone induction domain of Ste12p sufficient to mediate pheromone-induced transcription by these hybrid proteins. A minimal pheromone induction domain, delineated as residues 301 to 335 of Ste12p, is dependent on the pheromone mitogen-activated protein (MAP) kinase pathway for induction activity. Mutation of the three serine and threonine residues within the minimal pheromone induction domain did not affect transcriptional induction, indicating that the activity of this domain is not directly regulated by MAP kinase phosphorylation. By contrast, mutation of the two tyrosines or their preceding acidic residues led to a high level of transcriptional activity in the absence of pheromone and consequently to the loss of pheromone induction. This constitutively high activity was not affected by mutations in the MAP kinase cascade, suggesting that the function of the pheromone induction domain is normally repressed in the absence of pheromone. By two-hybrid analysis, this minimal domain interacts with two negative regulators, Dig1p and Dig2p (also designated Rst1p and Rst2p), and the interaction is abolished by mutation of the tyrosines. The pheromone induction domain itself has weak and inducible transcriptional activity, and its ability to potentiate transcription depends on the activity of an adjacent activation domain. These results suggest that the pheromone induction domain of Ste12p mediates transcriptional induction via a two-step process: the relief of repression and synergistic transcriptional activation with another activation domain.

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