Abstract
The amounts of normal and compensatory polyamines of polyamine-requiring Escherichia coli mutants grown in the absence of polyamines were determined. Although aminopropylcadaverine, a compensatory polyamine, was synthesized by MA135 (speB) and DR112 (speA speB), no aminopropylcadaverine or only small amounts of aminopropylcadaverine were synthesized by EWH319 (speA speB speC speD) and MA261 (speB speC), respectively. The average mass doubling times of MA135, DR112, MA261, and EWH319 grown in the absence of polyamines were 113, 105, 260, and 318 min, respectively. The correlation of these values with the sum of spermidine plus aminopropylcadaverine suggested that aminopropylcadaverine is important for cell growth in the presence of limiting amounts of normal polyamines. This hypothesis is supported by the results of aminopropylcadaverine stimulation of the in vitro synthesis of polyphenylalanine and MS2 RNA replicase and of its stimulation of the growth of MA261. For the following reasons, it was concluded that aminopropylcadaverine was synthesized preferentially from cadaverine made by ornithine decarboxylase: aminopropylcadaverine was synthesized in relatively large amounts in cells (MA135 and DR112) which possess ornithine decarboxylase; ornithine decarboxylase catalyzed the decarboxylation of lysine in vitro, and the in vivo formation of aminopropylcadaverine was inhibited by an inhibitor of ornithine decarboxylase.
MeSH Terms
Bacterial Proteins/biosynthesis
Cadaverine/analogs & derivatives,biosynthesis,metabolism,pharmacology
Carboxy-Lyases/analysis
Escherichia coli/genetics,growth & development,metabolism
Kinetics
Mutation
Ornithine Decarboxylase/analysis
Polyamines/analysis,biosynthesis
Chemicals
Bacterial Proteins
Polyamines
N-(3-aminopropyl)cadaverine
Carboxy-Lyases
Ornithine Decarboxylase
lysine decarboxylase
Cadaverine
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Igarashi K
Kashiwagi K
Hamasaki H
Miura A
Kakegawa T
Hirose S
Matsuzaki S
References (27)
27 references, click to expand
-
Isolation and characterization of a mutant of Escherichia coli blocked in the synthesis of putrescine.
J Bacteriol. 1970 Mar;101(3):725-30
PMID: 4908780
-
Infectivity of ribonucleic acid from tobacco mosaic virus.
Nature. 1956 Apr 14;177(4511):702-3
PMID: 13321939
-
Polyamine stimulation of nucleic acid synthesis in an uninfected and phage-infected polyamine auxotroph of Escherichia coli K12 (arginine-agmatine ureohydrolase-putrescine-spermidine-lysine-cadaverine).
Proc Natl Acad Sci U S A. 1972 Jan;69(1):213-7
PMID: 4550506
-
Purification and physical properties of inducible Escherichia coli lysine decarboxylase.
Biochemistry. 1974 Feb 12;13(4):662-70
PMID: 4590109
-
Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5'-phosphate binding site.
Biochemistry. 1974 Feb 12;13(4):670-6
PMID: 4204273
-
Growth of ribonucleic acid bacteriophage f2 in a conditional putrescine auxotroph of Escherichia coli: evidence for a polyamine role in translation.
J Bacteriol. 1974 Mar;117(3):1280-8
PMID: 4591952
-
Effect of polyamines of polyphenylalanine synthesis by Escherichia coli and rat-liver ribosomes.
Eur J Biochem. 1974 Oct 2;48(2):495-502
PMID: 4614977
-
Isolation, characterization, and mapping of Escherichia coli mutants blocked in the synthesis of ornithine decarboxylase.
J Bacteriol. 1975 Nov;124(2):791-9
PMID: 1102531
-
Comparison of the biosynthetic and biodegradative ornithine decarboxylases of Escherichia coli.
Biochemistry. 1977 Apr 19;16(8):1580-4
PMID: 15587
-
Decarboxylation of ornithine and lysine in rat tissues.
Biochim Biophys Acta. 1979 Jun 6;568(2):416-27
PMID: 486492
-
Mutants of Escherichia coli that do not contain 1,4-diaminobutane (putrescine) or spermidine.
J Biol Chem. 1979 Dec 25;254(24):12419-26
PMID: 159306
-
Structural specificity of the spermidine requirement of an Escherichia coli auxotroph.
J Bacteriol. 1980 Feb;141(2):456-63
PMID: 6154032
-
Lysine decarboxylase mutants of Escherichia coli: evidence for two enzyme forms.
J Bacteriol. 1980 Mar;141(3):1428-31
PMID: 6767710
-
Construction of an Escherichia coli strain unable to synthesize putrescine, spermidine, or cadaverine: characterization of two genes controlling lysine decarboxylase.
J Bacteriol. 1980 Dec;144(3):952-6
PMID: 7002915
-
Differential stimulation by polyamines of phage RNA-directed synthesis of proteins.
Biochim Biophys Acta. 1981 Dec 28;656(2):134-9
PMID: 7032595
-
Polyamine-deficient Neurospora crassa mutants and synthesis of cadaverine.
J Bacteriol. 1982 Oct;152(1):291-7
PMID: 6214545
-
DL-a-Monofluoromethylputrescine is a potent irreversible inhibitor of Escherichia coli ornithine decarboxylase.
Biochem J. 1982 Jun 15;204(3):771-5
PMID: 6812566
-
Putrescine and spermidine sensitivity of lysine decarboxylase in Escherichia coli: evidence for a constitutive enzyme and its mode of regulation.
Biochem Biophys Res Commun. 1983 Jul 29;114(2):882-8
PMID: 6349639
-
S-adenosylmethionine decarboxylase (Escherichia coli).
Methods Enzymol. 1983;94:228-30
PMID: 6353153
-
Structural specificity of the triamines sym-homospermidine and aminopropylcadaverine in stimulating growth of spermidine auxotrophs of Escherichia coli.
Biochem Biophys Res Commun. 1983 Dec 16;117(2):616-22
PMID: 6362672
-
Decreased protein-synthetic activity is an early consequence of spermidine depletion in rat hepatoma tissue-culture cells.
Biochem J. 1984 Feb 1;217(3):731-41
PMID: 6424650
-
Unusual polyamines in slime molds Physarum polycephalum and Dictyostelium discoideum.
J Biochem. 1984 Apr;95(4):1105-10
PMID: 6746590
-
Polyamines.
Annu Rev Biochem. 1984;53:749-90
PMID: 6206782
-
Physiological effects in bovine lymphocytes of inhibiting polyamine synthesis with ethylglyoxal bis(guanylhydrazone).
Cancer Res. 1984 Nov;44(11):5332-7
PMID: 6435867
-
Polyamines in microorganisms.
Microbiol Rev. 1985 Mar;49(1):81-99
PMID: 3157043
-
Protein measurement with the Folin phenol reagent.
J Biol Chem. 1951 Nov;193(1):265-75
PMID: 14907713
-
Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
Nature. 1970 Aug 15;227(5259):680-5
PMID: 5432063