On the control mechanism of bacterial growth by cyclic adenosine 3′, 5′-monophosphate

Inhibition of E. coli growth by cyclic adenosine monophosphate is observed in wild type strains cultured in glucose as carbon source, but not in a cyclic AMP receptor protein deficient mutant. A deletion mutant of the adenylate cyclase gene requires cyclic adenosine monophosphate for optimal growth....

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Autores principales: De Robertis Jr., E.M., Judewicz, N.D., Torres, H.N.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_0006291X_v55_n3_p758_DeRobertisJr
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spelling todo:paper_0006291X_v55_n3_p758_DeRobertisJr2023-10-03T14:04:06Z On the control mechanism of bacterial growth by cyclic adenosine 3′, 5′-monophosphate De Robertis Jr., E.M. Judewicz, N.D. Torres, H.N. adenylate cyclase cyclic amp bacterium cell division cell growth escherichia coli growth in vitro study microorganism theoretical study Adenylate Cyclase Cell Division Culture Media Cyclic AMP Enzyme Induction Escherichia coli Galactose Galactosidases Glucose Glycerol Glycosides Mutation Nitrosoguanidines Receptors, Drug Spectrophotometry Sulfhydryl Compounds Thiamine Time Factors Inhibition of E. coli growth by cyclic adenosine monophosphate is observed in wild type strains cultured in glucose as carbon source, but not in a cyclic AMP receptor protein deficient mutant. A deletion mutant of the adenylate cyclase gene requires cyclic adenosine monophosphate for optimal growth. Using glucose as carbon source, 2 mM cyclic AMP promotes maximal rates of cell multiplication in this mutant; however higher concentrations of the nucleotide inhibit growth. Cell multiplication of wild type strains grown in glycerol is not affected by cyclic adenosine monophosphate. Nevertheless, in this carbon source the growth rate of the adenylate cyclase mutant is strongly inhibited by concentrations of this nucleotide beyond 0.1 mM. This suggests that growth inhibition by exogenous cyclic adenosine monophosphate is highly dependent on the intracellular levels of the nucleotide. © 1973. Fil:De Robertis Jr., E.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Judewicz, N.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Torres, H.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_0006291X_v55_n3_p758_DeRobertisJr
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic adenylate cyclase
cyclic amp
bacterium
cell division
cell growth
escherichia coli
growth
in vitro study
microorganism
theoretical study
Adenylate Cyclase
Cell Division
Culture Media
Cyclic AMP
Enzyme Induction
Escherichia coli
Galactose
Galactosidases
Glucose
Glycerol
Glycosides
Mutation
Nitrosoguanidines
Receptors, Drug
Spectrophotometry
Sulfhydryl Compounds
Thiamine
Time Factors
spellingShingle adenylate cyclase
cyclic amp
bacterium
cell division
cell growth
escherichia coli
growth
in vitro study
microorganism
theoretical study
Adenylate Cyclase
Cell Division
Culture Media
Cyclic AMP
Enzyme Induction
Escherichia coli
Galactose
Galactosidases
Glucose
Glycerol
Glycosides
Mutation
Nitrosoguanidines
Receptors, Drug
Spectrophotometry
Sulfhydryl Compounds
Thiamine
Time Factors
De Robertis Jr., E.M.
Judewicz, N.D.
Torres, H.N.
On the control mechanism of bacterial growth by cyclic adenosine 3′, 5′-monophosphate
topic_facet adenylate cyclase
cyclic amp
bacterium
cell division
cell growth
escherichia coli
growth
in vitro study
microorganism
theoretical study
Adenylate Cyclase
Cell Division
Culture Media
Cyclic AMP
Enzyme Induction
Escherichia coli
Galactose
Galactosidases
Glucose
Glycerol
Glycosides
Mutation
Nitrosoguanidines
Receptors, Drug
Spectrophotometry
Sulfhydryl Compounds
Thiamine
Time Factors
description Inhibition of E. coli growth by cyclic adenosine monophosphate is observed in wild type strains cultured in glucose as carbon source, but not in a cyclic AMP receptor protein deficient mutant. A deletion mutant of the adenylate cyclase gene requires cyclic adenosine monophosphate for optimal growth. Using glucose as carbon source, 2 mM cyclic AMP promotes maximal rates of cell multiplication in this mutant; however higher concentrations of the nucleotide inhibit growth. Cell multiplication of wild type strains grown in glycerol is not affected by cyclic adenosine monophosphate. Nevertheless, in this carbon source the growth rate of the adenylate cyclase mutant is strongly inhibited by concentrations of this nucleotide beyond 0.1 mM. This suggests that growth inhibition by exogenous cyclic adenosine monophosphate is highly dependent on the intracellular levels of the nucleotide. © 1973.
format JOUR
author De Robertis Jr., E.M.
Judewicz, N.D.
Torres, H.N.
author_facet De Robertis Jr., E.M.
Judewicz, N.D.
Torres, H.N.
author_sort De Robertis Jr., E.M.
title On the control mechanism of bacterial growth by cyclic adenosine 3′, 5′-monophosphate
title_short On the control mechanism of bacterial growth by cyclic adenosine 3′, 5′-monophosphate
title_full On the control mechanism of bacterial growth by cyclic adenosine 3′, 5′-monophosphate
title_fullStr On the control mechanism of bacterial growth by cyclic adenosine 3′, 5′-monophosphate
title_full_unstemmed On the control mechanism of bacterial growth by cyclic adenosine 3′, 5′-monophosphate
title_sort on the control mechanism of bacterial growth by cyclic adenosine 3′, 5′-monophosphate
url http://hdl.handle.net/20.500.12110/paper_0006291X_v55_n3_p758_DeRobertisJr
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