scholarly journals Transcriptional regulation of the Kluyveromyces lactis beta-galactosidase gene.

1981 ◽  
Vol 1 (7) ◽  
pp. 629-634 ◽  
Author(s):  
L R Lacy ◽  
R C Dickson
Keyword(s):  
Protein Synthesis ◽  
Transcriptional Regulation ◽  
Enzyme Induction ◽  
Ribonucleic Acid ◽  
Molecular Basis ◽  
Kluyveromyces Lactis ◽  
Protein Synthesis Inhibitor ◽  
Synthesis Inhibitor ◽  
Messenger Ribonucleic Acid ◽  
Beta Galactosidase

We examined the molecular basis for beta-D-galactosidase (EC 3.2.1.23) induction in the yeast Kluyveromyces lactis. The protein synthesis inhibitor anisomycin effectively blocked both protein synthesis and enzyme induction by lactose. Further, hybridization analysis with the cloned beta-galactosidase gene indicated coordinate increases in the concentration of beta-galactosidase messenger ribonucleic acid and enzyme activity. The half-life of beta-galactosidase messenger ribonucleic acid was the same (4.8 +/- 0.4 min) when measured both before and at succeeding times during enzyme induction. These results strongly support the hypothesis that expression of the yeast beta-galactosidase gene is subject to transcriptional regulation.

Transcriptional regulation of the Kluyveromyces lactis beta-galactosidase gene

1981 ◽  
Vol 1 (7) ◽  
pp. 629-634
Author(s):  
L R Lacy ◽  
R C Dickson
Keyword(s):  
Protein Synthesis ◽  
Transcriptional Regulation ◽  
Enzyme Induction ◽  
Ribonucleic Acid ◽  
Molecular Basis ◽  
Kluyveromyces Lactis ◽  
Protein Synthesis Inhibitor ◽  
Synthesis Inhibitor ◽  
Messenger Ribonucleic Acid ◽  
Beta Galactosidase

We examined the molecular basis for beta-D-galactosidase (EC 3.2.1.23) induction in the yeast Kluyveromyces lactis. The protein synthesis inhibitor anisomycin effectively blocked both protein synthesis and enzyme induction by lactose. Further, hybridization analysis with the cloned beta-galactosidase gene indicated coordinate increases in the concentration of beta-galactosidase messenger ribonucleic acid and enzyme activity. The half-life of beta-galactosidase messenger ribonucleic acid was the same (4.8 +/- 0.4 min) when measured both before and at succeeding times during enzyme induction. These results strongly support the hypothesis that expression of the yeast beta-galactosidase gene is subject to transcriptional regulation.

scholarly journals Genetic regulation: yeast mutants constitutive for beta-galactosidase activity have an increased level of beta-galactosidase messenger ribonucleic acid.

1981 ◽  
Vol 1 (11) ◽  
pp. 1048-1056 ◽  
Author(s):  
R C Dickson ◽  
R M Sheetz ◽  
L R Lacy
Keyword(s):  
Ribonucleic Acid ◽  
Transcription Initiation ◽  
Regulatory Element ◽  
Kluyveromyces Lactis ◽  
Mrna Level ◽  
Genetic Regulation ◽  
Galactosidase Activity ◽  
Wild Type ◽  
Messenger Ribonucleic Acid ◽  
Beta Galactosidase

Mutants of Kluyveromyces lactis with elevated uninduced levels of beta-galactosidase (EC 32.1.2.3) activity, constitutive mutants (lac10c), were isolated and characterized to determine the basis for their constitutiveness. These lesions are not operator-type regulatory mutants because they are not closely linked to the beta-galactosidase structural gene. In a constitutive strain having a 7-fold increase in beta-galactosidase activity, the concentration of beta-galactosidase messenger ribonucleic acid (mRNA) was 8- to 10-fold higher than uninduced wild type. The half-life of beta-galactosidase mRNA was the same in the mutant strain (t1/2 = 4.5 +/- 0.2 min) as in uninduced wild-type cells (t1/2 = 4.8 +/- 0.1 min), indicating that the elevated mRNA level in the mutant was not due to a decreased rate of mRNA degradation. Consequently, we hypothesize that the LAC10 product regulates transcription of the beta-galactosidase gene; it probably affects the rate of transcription initiation. Parallel increases in enzyme protein, in constitutive levels of beta-galactosidase activity, and in mRNA further support this position, making translational or posttranslational control by LAC10 unlikely. Several types of data suggest that the LAC10 product functions as a negative regulatory element to prevent transcription. Other data demonstrate that lac10c mutations have pleiotrophic effects, there being constitutive levels not only of beta-galactosidase activity, but also the other lactose-inducible activities of galactokinase (EC 2.7.5.1), galactose-1-phosphate uridyl transferase (EC 2.7.7.10), and lactose transport. It would appear that LAC10 regulates lactose-inducible proteins.

Genetic regulation: yeast mutants constitutive for beta-galactosidase activity have an increased level of beta-galactosidase messenger ribonucleic acid

1981 ◽  
Vol 1 (11) ◽  
pp. 1048-1056
Author(s):  
R C Dickson ◽  
R M Sheetz ◽  
L R Lacy
Keyword(s):  
Ribonucleic Acid ◽  
Transcription Initiation ◽  
Regulatory Element ◽  
Kluyveromyces Lactis ◽  
Mrna Level ◽  
Genetic Regulation ◽  
Galactosidase Activity ◽  
Wild Type ◽  
Messenger Ribonucleic Acid ◽  
Beta Galactosidase

Mutants of Kluyveromyces lactis with elevated uninduced levels of beta-galactosidase (EC 32.1.2.3) activity, constitutive mutants (lac10c), were isolated and characterized to determine the basis for their constitutiveness. These lesions are not operator-type regulatory mutants because they are not closely linked to the beta-galactosidase structural gene. In a constitutive strain having a 7-fold increase in beta-galactosidase activity, the concentration of beta-galactosidase messenger ribonucleic acid (mRNA) was 8- to 10-fold higher than uninduced wild type. The half-life of beta-galactosidase mRNA was the same in the mutant strain (t1/2 = 4.5 +/- 0.2 min) as in uninduced wild-type cells (t1/2 = 4.8 +/- 0.1 min), indicating that the elevated mRNA level in the mutant was not due to a decreased rate of mRNA degradation. Consequently, we hypothesize that the LAC10 product regulates transcription of the beta-galactosidase gene; it probably affects the rate of transcription initiation. Parallel increases in enzyme protein, in constitutive levels of beta-galactosidase activity, and in mRNA further support this position, making translational or posttranslational control by LAC10 unlikely. Several types of data suggest that the LAC10 product functions as a negative regulatory element to prevent transcription. Other data demonstrate that lac10c mutations have pleiotrophic effects, there being constitutive levels not only of beta-galactosidase activity, but also the other lactose-inducible activities of galactokinase (EC 2.7.5.1), galactose-1-phosphate uridyl transferase (EC 2.7.7.10), and lactose transport. It would appear that LAC10 regulates lactose-inducible proteins.

Solubilization of a protein synthesis inhibitor from vaccinia virions.

1983 ◽  
Vol 45 (1) ◽  
pp. 452-455 ◽  
Author(s):  
F Ben-Hamida ◽  
A Person ◽  
G Beaud
Keyword(s):  
Protein Synthesis ◽  
Protein Synthesis Inhibitor ◽  
Synthesis Inhibitor

scholarly journals Effect of emetine, a protein synthesis inhibitor, on larval tail resorption in the ascidian Halocynthia roretzi

2006 ◽  
Vol 23 (2) ◽  
pp. 43-46
Author(s):  
Kiyotaka Matsumura ◽  
Manami Nagano ◽  
Sachiko Tsukamoto ◽  
Haruko Kato ◽  
Nobuhiro Fusetani
Keyword(s):  
Protein Synthesis ◽  
Protein Synthesis Inhibitor ◽  
Synthesis Inhibitor ◽  
Halocynthia Roretzi
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