Heterologous expression of the Saccharomyces cerevisiae alcohol acetyltransferase genes in Clostridium acetobutylicum and Escherichia coli for the production of isoamyl acetate

2003 ◽  
Vol 30 (7) ◽  
pp. 427-432 ◽  
Author(s):  
Catherine Emily Horton ◽  
Ke-Xue Huang ◽  
George N. Bennett ◽  
Frederick B. Rudolph
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Heterologous Expression ◽  
Clostridium Acetobutylicum ◽  
Isoamyl Acetate ◽  
Alcohol Acetyltransferase

scholarly journals The PLUTO plastidial nucleobase transporter also transports the thiamin precursor hydroxymethylpyrimidine

2018 ◽  
Vol 38 (2) ◽  
Author(s):  
Guillaume A.W. Beaudoin ◽  
Timothy S. Johnson ◽  
Andrew D. Hanson
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Root Growth ◽  
Heterologous Expression ◽  
Transporter Gene ◽  
Bacterial Genomes ◽  
Thiamin Biosynthesis ◽  
Increased Sensitivity ◽  
Arabidopsis Homolog

In plants, the hydroxymethylpyrimidine (HMP) and thiazole precursors of thiamin are synthesized and coupled together to form thiamin in plastids. Mutants unable to form HMP can be rescued by exogenous HMP, implying the presence of HMP transporters in the plasma membrane and plastids. Analysis of bacterial genomes revealed a transporter gene that is chromosomally clustered with thiamin biosynthesis and salvage genes. Its closest Arabidopsis homolog, the plastidic nucleobase transporter (PLUTO), is co-expressed with several thiamin biosynthetic enzymes. Heterologous expression of PLUTO in Escherichia coli or Saccharomyces cerevisiae increased sensitivity to a toxic HMP analog, and disrupting PLUTO in an HMP-requiring Arabidopsis line reduced root growth at low HMP concentrations. These data implicate PLUTO in plastidial transport and salvage of HMP.

Cellular Responses to Alcohol in Escherichia coli, Clostridium acetobutylicum, and Saccharomyces cerevisiae

2011 ◽  
Vol 49 (1) ◽  
pp. 105-108
Author(s):  
Ju-Yong Park ◽  
Chun-Sang Hong ◽  
Ji-Hye Han ◽  
Hyun-Woo Kang ◽  
Bong-Woo Chung ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Clostridium Acetobutylicum ◽  
Cellular Responses

Heterologous expression and purification of active L-asparaginase I of Saccharomyces cerevisiae in Escherichia coli host

2016 ◽  
Vol 33 (2) ◽  
pp. 416-424 ◽  
Author(s):  
João H. P. M. Santos ◽  
Iris M. Costa ◽  
João V. D. Molino ◽  
Mariana S. M. Leite ◽  
Marcela V. Pimenta ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Heterologous Expression ◽  
Expression And Purification

scholarly journals Balance of Activities of Alcohol Acetyltransferase and Esterase in Saccharomyces cerevisiae Is Important for Production of Isoamyl Acetate

1998 ◽  
Vol 64 (10) ◽  
pp. 4076-4078 ◽  
Author(s):  
Kiyoshi Fukuda ◽  
Nagi Yamamoto ◽  
Yoshifumi Kiyokawa ◽  
Toshiyasu Yanagiuchi ◽  
Yoshinori Wakai ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Enzyme Activities ◽  
Isoamyl Alcohol ◽  
Isoamyl Acetate ◽  
Small Scale ◽  
Alcohol Acetyltransferase ◽  
Yeast Strains ◽  
Acetate Accumulation ◽  
Esterase Gene ◽  
Optimum Production

ABSTRACT Isoamyl acetate is synthesized from isoamyl alcohol and acetyl coenzyme A by alcohol acetyltransferase (AATFase) inSaccharomyces cerevisiae and is hydrolyzed by esterases at the same time. We hypothesized that the balance of both enzyme activities was important for optimum production of isoamyl acetate in sake brewing. To test this hypothesis, we constructed yeast strains with different numbers of copies of the AATFase gene (ATF1) and the isoamyl acetate-hydrolyzing esterase gene (IAH1) and used these strains in small-scale sake brewing. Fermentation profiles as well as components of the resulting sake were largely alike; however, the amount of isoamyl acetate in the sake increased with an increasing ratio of AATFase/Iah1p esterase activity. Therefore, we conclude that the balance of these two enzyme activities is important for isoamyl acetate accumulation in sake mash.

Microbe Engineering of Guaia-6,10(14)-diene as a Building Block for the Semisynthetic Production of Plant-Derived (−)-Englerin A

2019 ◽  
Author(s):  
Thomas Siemon ◽  
Zhangqian Wang ◽  
Guangkai Bian ◽  
Tobias Seitz ◽  
Ziling Ye ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Synthetic Biology ◽  
Chemical Synthesis ◽  
Building Block ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Economical Method ◽  
Englerin A ◽  
Transient Receptor

Herein, we report the semisynthetic production of the potent transient receptor potential canonical (TRPC) channel agonist (−)-englerin A (EA), using guaia-6,10(14)-diene as the starting material. Guaia-6,10(14)-diene was systematically engineered in Escherichia coli and Saccharomyces cerevisiae using the CRISPR/Cas9 system and produced with high titers. This provided us the opportunity to execute a concise chemical synthesis of EA and the two related guaianes (−)-oxyphyllol and (+)-orientalol E. The potentially scalable approach combines the advantages of synthetic biology and chemical synthesis and provides an efficient and economical method for producing EA as well as its analogs.

Microbe Engineering of Guaia-6,10(14)-diene as a Building Block for the Semisynthetic Production of Plant-Derived (−)-Englerin A

2019 ◽  
Author(s):  
Thomas Siemon ◽  
Zhangqian Wang ◽  
Guangkai Bian ◽  
Tobias Seitz ◽  
Ziling Ye ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Saccharomyces Cerevisiae ◽  
Synthetic Biology ◽  
Chemical Synthesis ◽  
Building Block ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Economical Method ◽  
Englerin A ◽  
Transient Receptor

Herein, we report the semisynthetic production of the potent transient receptor potential canonical (TRPC) channel agonist (−)-englerin A (EA), using guaia-6,10(14)-diene as the starting material. Guaia-6,10(14)-diene was systematically engineered in Escherichia coli and Saccharomyces cerevisiae using the CRISPR/Cas9 system and produced with high titers. This provided us the opportunity to execute a concise chemical synthesis of EA and the two related guaianes (−)-oxyphyllol and (+)-orientalol E. The potentially scalable approach combines the advantages of synthetic biology and chemical synthesis and provides an efficient and economical method for producing EA as well as its analogs.

Yeast dom34 Mutants Are Defective in Multiple Developmental Pathways and Exhibit Decreased Levels of Polyribosomes

Genetics ◽  
1998 ◽  
Vol 149 (1) ◽  
pp. 45-56
Author(s):  
Luther Davis ◽  
JoAnne Engebrecht
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Heterologous Expression ◽  
Protein Translation ◽  
Developmental Pathways ◽  
G1 Phase ◽  
Growth Defect ◽  
Wild Type ◽  
Drosophila Homolog ◽  
Mutant Cells

Abstract The DOM34 gene of Saccharomyces cerevisiae is similar togenes found in diverse eukaryotes and archaebacteria. Analysis of dom34 strains shows that progression through the G1 phase of the cell cycle is delayed, mutant cells enter meiosis aberrantly, and their ability to form pseudohyphae is significantly diminished. RPS30A, which encodes ribosomal protein S30, was identified in a screen for high-copy suppressors of the dom34Δ growth defect. dom34Δ mutants display an altered polyribosome profile that is rescued by expression of RPS30A. Taken together, these data indicate that Dom34p functions in protein translation to promote G1 progression and differentiation. A Drosophila homolog of Dom34p, pelota, is required for the proper coordination of meiosis and spermatogenesis. Heterologous expression of pelota in dom34Δ mutants restores wild-type growth and differentiation, suggesting conservation of function between the eukaryotic members of the gene family.

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