The Participation of Ornithine and Citrulline in the Regulation of Arginine Metabolism in Saccharomyces cerevisiae

1970 ◽  
Vol 12 (1) ◽  
pp. 40-47 ◽  
Author(s):  
F. Ramos ◽  
P. Thuriaux ◽  
J. M. Wiame ◽  
J. Bechet
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Arginine Metabolism

scholarly journals Regulation of arginine metabolism in Saccharomyces cerevisiae. Association of arginase and ornithine transcarbamoylase.

1986 ◽  
Vol 261 (27) ◽  
pp. 12814-12819 ◽  
Author(s):  
E Eisenstein ◽  
L T Duong ◽  
R L Ornberg ◽  
J C Osborne ◽  
P Hensley
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Arginine Metabolism ◽  
Ornithine Transcarbamoylase

scholarly journals Genetic evidence for a role for MCM1 in the regulation of arginine metabolism in Saccharomyces cerevisiae.

1993 ◽  
Vol 13 (4) ◽  
pp. 2586-2592 ◽  
Author(s):  
F Messenguy ◽  
E Dubois
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Arginine Metabolism ◽  
In Vitro Binding ◽  
Catabolic Enzymes ◽  
Catabolic Genes ◽  
Vitro Binding ◽  
Regulatory Complex ◽  
Cell Type Specific

ARGRI, ARGRII, and ARGRIII regulatory proteins control the expression of arginine anabolic and catabolic genes in Saccharomyces cerevisiae. We have shown that MCM1 is part of the ARGR regulatory complex, by in vitro binding experiments, at the ARGR5,6 promoter. The participation of MCM1 in the regulation of arginine metabolism is confirmed by the behavior of an mcm1-gcn4 mutant, which is affected in the repression of arginine anabolic genes. In this mcm1 mutant, synthesis of the catabolic enzymes is rather constitutive, but this derepression requires the integrity of the ARGR system and of the target sequences of these proteins in the CAR1 promoter. Our in vitro binding experiments confirm the presence of MCM1 in the protein complex interacting with the promoters of the catabolic CAR1 and CAR2 genes. This is the first in vivo transcription role ascribed to MCM1 other than its role in the transcription of cell-type-specific genes.

scholarly journals In vitro studies of the binding of the ARGR proteins to the ARG5,6 promoter.

1991 ◽  
Vol 11 (4) ◽  
pp. 2162-2168 ◽  
Author(s):  
E Dubois ◽  
F Messenguy
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Specific Binding ◽  
Regulatory Element ◽  
Regulatory Proteins ◽  
Arginine Metabolism ◽  
Mobility Shift ◽  
Catabolic Genes ◽  
Gel Mobility Shift ◽  
Dna Complex

ARGRI, ARGRII, and ARGRIII regulatory proteins control the expression of arginine anabolic and catabolic genes in Saccharomyces cerevisiae. We show here that they are also required in vitro to observe a protein-DNA complex with the promoter of the ARG5,6 gene. The specific binding of ARGR proteins in vitro is stimulated by arginine. Antibodies raised against a synthetic MCM1 polypeptide retard the migration of ARGR-DNA complex on gel mobility shift assays. This result suggests that MCM1 could be an additional regulatory element of arginine metabolism.

In vitro studies of the binding of the ARGR proteins to the ARG5,6 promoter

1991 ◽  
Vol 11 (4) ◽  
pp. 2162-2168
Author(s):  
E Dubois ◽  
F Messenguy
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Specific Binding ◽  
Regulatory Element ◽  
Regulatory Proteins ◽  
Arginine Metabolism ◽  
Mobility Shift ◽  
Catabolic Genes ◽  
Gel Mobility Shift ◽  
Dna Complex

ARGRI, ARGRII, and ARGRIII regulatory proteins control the expression of arginine anabolic and catabolic genes in Saccharomyces cerevisiae. We show here that they are also required in vitro to observe a protein-DNA complex with the promoter of the ARG5,6 gene. The specific binding of ARGR proteins in vitro is stimulated by arginine. Antibodies raised against a synthetic MCM1 polypeptide retard the migration of ARGR-DNA complex on gel mobility shift assays. This result suggests that MCM1 could be an additional regulatory element of arginine metabolism.

scholarly journals Metabolic Engineering of Saccharomyces cerevisiae for Production of Novel Cyanophycins with an Extended Range of Constituent Amino Acids

2009 ◽  
Vol 75 (11) ◽  
pp. 3437-3446 ◽  
Author(s):  
Anna Steinle ◽  
Klaus Bergander ◽  
Alexander Steinbüchel
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Ornithine Carbamoyltransferase ◽  
Argininosuccinate Synthetase ◽  
Argininosuccinate Lyase ◽  
Arginine Metabolism ◽  
Extended Range ◽  
Putative Precursor ◽  
Cyanophycin Synthetase

ABSTRACT Cyanophycin (multi-l-arginyl-poly-l-aspartic acid; also known as cyanophycin grana peptide [CGP]) is a putative precursor for numerous biodegradable technically used chemicals. Therefore, the biosynthesis and production of the polymer in recombinant organisms is of special interest. The synthesis of cyanophycin derivatives consisting of a wider range of constituents would broaden the applications of this polymer. We applied recombinant Saccharomyces cerevisiae strains defective in arginine metabolism and expressing the cyanophycin synthetase of Synechocystis sp. strain PCC 6308 in order to synthesize CGP with citrulline and ornithine as constituents. Strains defective in arginine degradation (Car1 and Car2) accumulated up to 4% (wt/wt) CGP, whereas strains defective in arginine synthesis (Arg1, Arg3, and Arg4) accumulated up to 15.3% (wt/wt) of CGP, which is more than twofold higher than the previously content reported in yeast and the highest content ever reported in eukaryotes. Characterization of the isolated polymers by different analytical methods indicated that CGP synthesized by strain Arg1 (with argininosuccinate synthetase deleted) consisted of up to 20 mol% of citrulline, whereas CGP from strain Arg3 (with ornithine carbamoyltransferase deleted) consisted of up to 8 mol% of ornithine, and CGP isolated from strain Arg4 (with argininosuccinate lyase deleted) consisted of up to 16 mol% lysine. Cultivation experiments indicated that the incorporation of citrulline or ornithine is enhanced by the addition of low amounts of arginine (2 mM) and also by the addition of ornithine or citrulline (10 to 40 mM), respectively, to the medium.

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