Abstract
Mutants defective in the conversion of arginine to putrescine were found by screening clones from mutagenized cultures for inability to produce urea during growth in arginine-supplemented media. Two partially blocked mutants were isolated; one was deficient in arginine decarboxylase and the other was deficient in agmatine ureohydrolase. As predicted from the pattern of putrescine synthesis in Escherichia coli, these mutants were conditionally putrescine-deficient. When grown in either minimal or ornithine-supplemented media, conditions which lead to preferential utilization of the ornithine to putrescine pathway, the mutants had normal intracellular polyamine levels. However, when the mutants were placed in arginine-supplemented media, the level of intracellular putrescine was lowered markedly. Under conditions where intracellular putrescine was 1% of normal, the doubling time of the mutants was increased approximately 10%. The putrescine-deficient mutants had wild-type morphology, normal levels of protein and ribonucleic acid (RNA), and stringent amino acid control of RNA synthesis.
Full text
PDF![731](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab07/250385/b492062c02f6/jbacter00384-0105.png)
![732](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab07/250385/698a1fe2fe5c/jbacter00384-0106.png)
![733](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab07/250385/d121f4587841/jbacter00384-0107.png)
![734](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab07/250385/442e22c7087f/jbacter00384-0108.png)
![735](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab07/250385/4762c5ac72b0/jbacter00384-0109.png)
![736](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab07/250385/8765e611380b/jbacter00384-0110.png)
![737](https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ab07/250385/a02ed85273e7/jbacter00384-0111.png)
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- AMES B. N., DUBIN D. T. The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J Biol Chem. 1960 Mar;235:769–775. [PubMed] [Google Scholar]
- AMES B. N., GARRY B., HERZENBERG L. A. The genetic control of the enzymes of histidine biosynthesis in Salmonella typhimurium. J Gen Microbiol. 1960 Apr;22:369–378. doi: 10.1099/00221287-22-2-369. [DOI] [PubMed] [Google Scholar]
- Abraham K. A. Studies on DNA-dependent RNA polymerase from Escherichia coli. 1. The mechanism of polyamine induced stimulation of enzyme activity. Eur J Biochem. 1968 Jun;5(1):143–146. doi: 10.1111/j.1432-1033.1968.tb00348.x. [DOI] [PubMed] [Google Scholar]
- BRETTHAUER R. K., MARCUS L., CHALOUPKA J., HALVORSON H. O., BOCK R. M. AMINO ACID INCORPORATION INTO PROTEIN BY CELL-FREE EXTRACTS OF YEAST. Biochemistry. 1963 Sep-Oct;2:1079–1084. doi: 10.1021/bi00905a029. [DOI] [PubMed] [Google Scholar]
- COHEN S. S., LICHTENSTEIN J. Polyamines and ribosome structure. J Biol Chem. 1960 Jul;235:2112–2116. [PubMed] [Google Scholar]
- COLBOURN J. L., WITHERSPOON B. H., HERBST E. J. Effect of intracellular spermine on ribosomes of Escherichia coli. Biochim Biophys Acta. 1961 May 13;49:422–424. doi: 10.1016/0006-3002(61)90155-x. [DOI] [PubMed] [Google Scholar]
- Choi Y. S., Carr C. W. Ion-binding studies of ribonucleic acid and Escherichia coli ribosomes. J Mol Biol. 1967 Apr 28;25(2):331–345. doi: 10.1016/0022-2836(67)90145-3. [DOI] [PubMed] [Google Scholar]
- DUBIN D. T., ROSENTHAL S. M. The acetylation of polyamines in Escherichia coli. J Biol Chem. 1960 Mar;235:776–782. [PubMed] [Google Scholar]
- Ezekiel D. H., Brockman H. Effect of spermidine treatment on amino acid availability in amino acid-starved Escherichia coli. J Mol Biol. 1968 Feb 14;31(3):541–552. doi: 10.1016/0022-2836(68)90426-9. [DOI] [PubMed] [Google Scholar]
- FELSENFELD G., HUANG S. L. Some effects of charge and structure upon ionic interactions of nucleic acids. Biochim Biophys Acta. 1961 Jul 22;51:19–32. doi: 10.1016/0006-3002(61)91012-5. [DOI] [PubMed] [Google Scholar]
- FOX C. F., WEISS S. B. ENZYMATIC SYNTHESIS OF RIBONUCLEIC ACID. II. PROPERTIES OF THE DEOXYRIBONUCLEIC ACID-PRIMED REACTION WITH MICROCOCCUS LYSODEIKTICUS RIBONUCLEIC ACID POLYMERASE. J Biol Chem. 1964 Jan;239:175–185. [PubMed] [Google Scholar]
- GORINI L., GUNDERSEN W., BURGER M. Genetics of regulation of enzyme synthesis in the arginine biosynthetic pathway of Escherichia coli. Cold Spring Harb Symp Quant Biol. 1961;26:173–182. doi: 10.1101/sqb.1961.026.01.022. [DOI] [PubMed] [Google Scholar]
- GORINI L., KAUFMAN H. Selecting bacterial mutants by the penicillin method. Science. 1960 Feb 26;131(3400):604–605. doi: 10.1126/science.131.3400.604. [DOI] [PubMed] [Google Scholar]
- Gale E. F. The production of amines by bacteria: The decarboxylation of amino-acids by strains of Bacterium coli. Biochem J. 1940 Mar;34(3):392–413. doi: 10.1042/bj0340392. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HAROLD F. M. STABILIZATION OF STREPTOCOCCUS FAECALIS PROTOPLASTS BY SPERMINE. J Bacteriol. 1964 Nov;88:1416–1420. doi: 10.1128/jb.88.5.1416-1420.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
- HERBST E. J., GLINOS E. B., AMUNDSEN L. H. An analysis of the putrescine requirement of Hemophilus parainfluenzae. J Biol Chem. 1955 May;214(1):175–184. [PubMed] [Google Scholar]
- HERBST E. J., WEAVER R. H., KEISTER D. L. The gram reaction and cell composition: diamines and polyamines. Arch Biochem Biophys. 1958 May;75(1):171–177. doi: 10.1016/0003-9861(58)90407-7. [DOI] [PubMed] [Google Scholar]
- HERSHKO A., AMOZ S., MAGER J. Effect of polyamines and divalent metals on in vitro incorporation of amino acids into ribonucleoprotein particles. Biochem Biophys Res Commun. 1961 May 15;5:46–51. doi: 10.1016/0006-291x(61)90078-x. [DOI] [PubMed] [Google Scholar]
- Hirschman S., Leng M., Felsenfield G. Interaction of spermine and DNA. Biopolymers. 1967 Feb;5(2):227–233. doi: 10.1002/bip.1967.360050209. [DOI] [PubMed] [Google Scholar]
- Hirshfield I. N., Rosenfeld H. J., Leifer Z., Maas W. K. Isolation and characterization of a mutant of Escherichia coli blocked in the synthesis of putrescine. J Bacteriol. 1970 Mar;101(3):725–730. doi: 10.1128/jb.101.3.725-730.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hunninghake D., Grisolia S. A sensitive and convenient micromethod for estimation of urea, citrulline, and carbamyl derivatives. Anal Biochem. 1966 Aug;16(2):200–205. doi: 10.1016/0003-2697(66)90147-3. [DOI] [PubMed] [Google Scholar]
- KRAKOW J. S. RIBONUCLEIC ACID POLYMERASE OF AZOTOBACTER VINELANDII. III. EFFECT OF POLYAMINES. Biochim Biophys Acta. 1963 Aug 20;72:566–571. [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- MAAS W. K. Studies on repression of arginine biosynthesis in Escherichia coli. Cold Spring Harb Symp Quant Biol. 1961;26:183–191. doi: 10.1101/sqb.1961.026.01.023. [DOI] [PubMed] [Google Scholar]
- MAGER J. Influence of osmotic pressure on the polyamine requirement of Neisseria perflava and Pasteurella tularensis for growth in defined media. Nature. 1955 Nov 12;176(4489):933–934. doi: 10.1038/176933a0. [DOI] [PubMed] [Google Scholar]
- MAGER J. Spermine as a protective agent against osmotic lysis. Nature. 1959 Jun 27;183:1827–1828. doi: 10.1038/1831827a0. [DOI] [PubMed] [Google Scholar]
- MAGER J. The stabilizing effect of spermine and related polyamines and bacterial protoplasts. Biochim Biophys Acta. 1959 Dec;36:529–531. doi: 10.1016/0006-3002(59)90195-7. [DOI] [PubMed] [Google Scholar]
- MOLLER M. L., KIM K. EFFECTS OF PUTRESCINE AND MAGNESIUM ON THE RIBOSOMES OF A PSEUDOMONAS. Biochem Biophys Res Commun. 1965 Jun 18;20:46–52. doi: 10.1016/0006-291x(65)90948-4. [DOI] [PubMed] [Google Scholar]
- Mills J., Dubin D. T. Some effects of spermine on Escherichia coli. Mol Pharmacol. 1966 Jul;2(4):311–318. [PubMed] [Google Scholar]
- Morris D. R., Koffron K. L. Putrescine biosynthesis in Escherichia coli. Regulation through pathway selection. J Biol Chem. 1969 Nov 25;244(22):6094–6099. [PubMed] [Google Scholar]
- Morris D. R., Koffron K. L. Urea production and putrescine biosynthesis by Escherichia coli. J Bacteriol. 1967 Nov;94(5):1516–1519. doi: 10.1128/jb.94.5.1516-1519.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Morris D. R., Pardee A. B. A biosynthetic ornithine decarboxylase in Escherichia coli. Biochem Biophys Res Commun. 1965 Sep 22;20(6):697–702. doi: 10.1016/0006-291x(65)90072-0. [DOI] [PubMed] [Google Scholar]
- NOVICK R. P., MAAS W. K. Control by endogenously synthesized arginine of the formation of ornithine transcarbamylase in Escherichia coli. J Bacteriol. 1961 Feb;81:236–240. doi: 10.1128/jb.81.2.236-240.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Petersen E. E., Kröger H., Hagen U. The influence of spermidine on the reaction of RNA nucleotidyltransferase. Biochim Biophys Acta. 1968 Jul 23;161(2):325–330. doi: 10.1016/0005-2787(68)90110-x. [DOI] [PubMed] [Google Scholar]
- RAZIN S., ROZANSKY R. Mechanism of the antibacterial action of spermine. Arch Biochem Biophys. 1959 Mar;81(1):36–54. doi: 10.1016/0003-9861(59)90173-0. [DOI] [PubMed] [Google Scholar]
- ROGOSA M., BISHOP F. S. THE GENUS VEILLONELLA . II. NUTRITIONAL STUDIES. J Bacteriol. 1964 Mar;87:574–580. doi: 10.1128/jb.87.3.574-580.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stevens L., Morrison M. R. Studies on the role of polyamines associated with the ribosomes from Bacillus stearothermophilus. Biochem J. 1968 Jul;108(4):633–640. doi: 10.1042/bj1080633. [DOI] [PMC free article] [PubMed] [Google Scholar]
- TABOR C. W., ROSENTHAL S. M. Pharmacology of spermine and spermidine; some effects on animals and bacteria. J Pharmacol Exp Ther. 1956 Feb;116(2):139–155. [PubMed] [Google Scholar]
- TABOR H., ROSENTHAL S. M., TABOR C. W. The biosynthesis of spermidine and spermine from putrescine and methionine. J Biol Chem. 1958 Oct;233(4):907–914. [PubMed] [Google Scholar]
- TABOR H., TABOR C. W. SPERMIDINE, SPERMINE, AND RELATED AMINES. Pharmacol Rev. 1964 Sep;16:245–300. [PubMed] [Google Scholar]
- TABOR H. The protective effect of spermine and other polyamines against heat denaturation of deoxyribonucleic acid. Biochemistry. 1962 May 25;1:496–501. doi: 10.1021/bi00909a021. [DOI] [PubMed] [Google Scholar]
- Tabor C. W., Kellogg P. D. The effect of isolation conditions on the polyamine content of Escherichia coli ribosomes. J Biol Chem. 1967 Mar 10;242(5):1044–1052. [PubMed] [Google Scholar]
- Tabor C. W. STABILIZATION OF PROTOPLASTS AND SPHEROPLASTS BY SPERMINE AND OTHER POLYAMINES. J Bacteriol. 1962 May;83(5):1101–1111. doi: 10.1128/jb.83.5.1101-1111.1962. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tabor H., Tabor C. W. Formation of 1,4-diaminobutane and of spermidine by an ornithine auxotroph of Escherichia coli grown on limiting ornithine or arginine. J Biol Chem. 1969 May 10;244(9):2286–2292. [PubMed] [Google Scholar]
- Takeda Y. Polyamines and protein synthesis. II. The shift in optimal concentration of Mg2+ by polyamines in the MS2 phage RNA-directed polypeptide synthesis. Biochim Biophys Acta. 1969 Mar 18;179(1):232–234. doi: 10.1016/0005-2787(69)90140-3. [DOI] [PubMed] [Google Scholar]
- VOGEL H. J. Aspects of repression in the regulation of enzyme synthesis: pathway-wide control and enzyme-specific response. Cold Spring Harb Symp Quant Biol. 1961;26:163–172. doi: 10.1101/sqb.1961.026.01.021. [DOI] [PubMed] [Google Scholar]
- VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
- VYAS S., MAAS W. K. Feedback inhibition of acetylglutamate synthetase by arginine in Escherichia coli. Arch Biochem Biophys. 1963 Mar;100:542–546. doi: 10.1016/0003-9861(63)90124-3. [DOI] [PubMed] [Google Scholar]
- WEAVER R. H., HERBST E. J. Metabolism of diamines and polyamines in microorganisms. J Biol Chem. 1958 Apr;231(2):637–646. [PubMed] [Google Scholar]