Regulation of Polyamine Biosynthesis in Escherichia coli by Basic Proteins

In Escherichia coli, the biosynthetic ornithine and arginine decarboxylases (EC 4.1.1.17 and 4.1.1.19, respectively) are responsible for the biosynthesis of polyamines from ornithine and arginine, respectively. When E. coli cells are grown in the presence of increasing amounts of polyamines, a progr...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1983-09, Vol.80 (17), p.5181-5184
Main Authors: Heller, John S., Rostomily, Robert, Kyriakidis, Dimitri A., Canellakis, Evangelos S.
Format: Article
Language:English
Subjects:
Amino acids
Amino Acids - analysis
Arginine - metabolism
Biochemistry
Biosynthesis
Carboxy-Lyases - genetics
Carboxy-Lyases - metabolism
Cell growth
DNA-binding protein
Enzymes
Escherichia coli
Escherichia coli - enzymology
Fractions
histone H2B
Histones
Histones - genetics
Ornithine - metabolism
Ornithine Decarboxylase - genetics
Ornithine Decarboxylase - metabolism
Polyamines
Polyamines - biosynthesis
Titration
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Summary:In Escherichia coli, the biosynthetic ornithine and arginine decarboxylases (EC 4.1.1.17 and 4.1.1.19, respectively) are responsible for the biosynthesis of polyamines from ornithine and arginine, respectively. When E. coli cells are grown in the presence of increasing amounts of polyamines, a progressive increase in the amount of antizyme 1 and antizyme 2 occurs. The amino acid compositions of antizymes 1 and 2 show them to be basic proteins; antizyme 1 has an amino acid composition similar to that of the E. coli histone-like protein HU and of the eukaryotic histone H2B; antizyme 2 is characterized by an unusually high arginine content. We find these proteins to be specific inhibitors of both the biosynthetic ornithine decarboxylase and the biosynthetic arginine decarboxylase. They do not inhibit the corresponding biodegradative ornithine and arginine decarboxylases, nor do they inhibit lysine decarboxylase or S-adenosylmethionine decarboxylase. These properties of the antizymes favor their function in the regulation of polyamine biosynthesis in E. coli. The ability of the purified antizymes to inhibit the ornithine and arginine decarboxylases is stabilized in acidic buffers and is lost upon prolonged exposure to solutions at neutral or basic pH.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.80.17.5181