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Tetrapyrrole biosynthesis: N-methyl-N′-nitrosoguanidine-induced mutants of Propionibacterium shermanii

Published online by Cambridge University Press:  14 April 2009

N. H. Georgopapadakou ,
J. Petrillo ,
A. I. Scott  and
B. Low
N. H. Georgopapadakou
Affiliation:
Chemistry Department, Yale University, New Haven, Connecticut 06520
J. Petrillo
Affiliation:
Chemistry Department, Yale University, New Haven, Connecticut 06520
A. I. Scott
Affiliation:
Chemistry Department, Yale University, New Haven, Connecticut 06520
B. Low
Affiliation:
Radiobiology Laboratories, Yale University School of Medicine, New Haven, Connecticut 06510
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Summary

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An isolation method for N-methyl-N′-nitrosoguanidine-induced catalase negative mutants of P. shermanii based on replica plating is described. In contrast to previous methods, it extends to the early stages of tetrapyrrole biosynthesis which are common in both corrins and porphyrins. It may thus aid in elucidating the mechanism and control of porphyrin and corrin biosynthesis. Some preliminary results are discussed.

Type
Short Papers
Information
Genetics Research , Volume 28 , Issue 1 , August 1976 , pp. 93 - 100
Copyright
Copyright © Cambridge University Press 1976

References

REFERENCES

Adelberg, E. A., Mandel, M. & Ching Chen, G. C. (1965). Optimal conditions for mutagenesis by N-methyl-N′-nitrosoguanidine in Escherichia coli K·12. Biochemical and Biophysical Research Communications 18, 788–795.CrossRefGoogle Scholar
Abkad'eva, Z. A. & Kalenik, N. M. (1971). Physiological and biochemical characteristics of some mutants of Propionibaclerium shermanii. Microbiologiya 40, 880–885.Google Scholar
Bogorad, L. (1958 a). The enzymatic synthesis of porphyrins from porphobilinogen. I. Uroporphyrin I. Journal of Biological Chemistry 233, 501–509.CrossRefGoogle ScholarPubMed
Bogorad, L. (1958 b). The enzymatic synthesis of porphyrins from porphobilinogen. II. Uroporphyrin III. Journal of Biological Chemistry 233, 510–515.CrossRefGoogle ScholarPubMed
Bykhovskii, V. Ya., Zaitseva, N. I. & Bukin, U. N. (1969). Some aspects of the regulation of vitamin B12 and porphyrin biosynthesis in Propionibacterium shermanii. Doklady Akademii Nauk. SSSR 185, 459–461.Google Scholar
De Vries, W., Van Wijck-Kapteijn, W. M. C. & Stouthamer, A. H. (1972). Influence of oxygen on growth, cytochrome synthesis and fermentation pattern in propionic acid bacteria. Journal of General Microbiology 71, 515–524.CrossRefGoogle ScholarPubMed
Falk, J. E. (1964). Porphyrins and Metalloporphyrins, New York: Elsevier.Google Scholar
Frank, B., Gantz, D. & Hüper, F. (1972). Total synthesis of [α,γ-14C2] uroporphyrin III. Angewandte Chemie International Edition in English, 11, 420.CrossRefGoogle Scholar
Friedman, H. C. (1975). Biosynthesis of corrinoids. In Cobalamin: Biochemistry and Pathology (ed. Babior, B. M.), pp. 77–89. New York: Wiley.Google Scholar
Granick, S. & Mauzerall, D. (1958). Enzymic formation of protoporphyrin from coproporphyrinogen III. Federation Proceedings 17, 233.Google Scholar
Guerola, N., Ingraham, J. L. & Cerda-Oimedo, E. (1971). Induction of closely linked multiple mutations by nitrosoquanidine. Nature New Biology 230, 122–123.CrossRefGoogle Scholar
Hoare, D. S. & Heath, H. (1959). The biosynthesis of porphyrins from porphobilinogen by Rhodopseudomanas spheroides. Biochemical Journal 73, 679–690.CrossRefGoogle Scholar
Lederberg, J. & Lederberg, E. M. (1952). Replica plating and indirect selection of bacterial mutants. Journal of Bacteriology 63, 399–406.CrossRefGoogle ScholarPubMed
Low, B. (1973). Rapid mapping of conditional and auxotrophic mutations in Escherichia coli K-12. Journal of Bacteriology 113, 798–812.CrossRefGoogle ScholarPubMed
Mashur, V. A., Vorob'eva, L. I. & Iordan, E. P. (1971). Fermentation caused by a mutant of propionic acid bacteria that do not form B12 coenzymes. Prikladnaya Biokhimiya Mikrobiologiya 7, 552–555.Google Scholar
Menon, A. I. & Shemin, D. (1967). Concomitant decrease of enzymic activities concerned with the synthesis of coenzyme B12 and of propionic acid in Propionibacteria. Archives of Biochemistry of Biophysics 121, 304–310.CrossRefGoogle Scholar
Pedziwilk, F. (1971). Ethyl methanesulfonate (EMS-induced mutants of Propionibacterium Shermanii. Acta Microbiologica Polinica B 3, 79–89.Google ScholarPubMed
Porra, R. J. & Jones, O. T. G. (1963). Studies in ferrochelatase. 1. Assay and properties of ferrochelotase from a pig-liver mitochondrial extract. Biochemical Journal 87, 181–185.CrossRefGoogle ScholarPubMed
Sasarman, A., Subdeanu, M., Szegli, G., Horodniceanu, T., Greceanu, V. & Dumitrescu, A. (1968). Hemin-deficient mutants of Escherichia coli K-12. Journal of Bacteriology 96, 570–572.CrossRefGoogle ScholarPubMed
Sato, K., Shimizu, S. & Fukui, S. (1971). Studies on the corinoids and porphyrins in Streptomycetes. V. Effect of additions on porphyrin excretion and σ-aminolevulinic acid dehydratase in Streptomyces olivaceus. Agr. Biol. Chem. 35, 344–350.CrossRefGoogle Scholar
Scott, A. I. (1975). Concerning the biosynthesis of vitamin B12. Annals of the New York Academy of Sciences 244, 356–370.CrossRefGoogle ScholarPubMed
Tarlton, E. J., MacDonald, S. F. & Baltazzi, E. (1960). Uroporphyrin 3. Journal of the American Chemical Society 82, 4389.CrossRefGoogle Scholar
Tien, W. & White, D. C. (1968). Linear sequential arrangement of genes for the biosynthetic pathway of protoheme in Staphylococcus aureus. Proceedings of the National Academy of Sciences, U.S.A. 61, 1392–1398.CrossRefGoogle ScholarPubMed
Tuboi, S., Kim, H. J. & Kikuchi, G. (1970). Occurrence and properties of two types of σ-aminolevulinate synthetase in Rhodopscudomonas spheroides. Archives of Biochemistry & Biophysics 138, 147–159.CrossRefGoogle Scholar
Vorob'eva, L. I., Baranova, N. A. & Thanh, C. T. (1973). Mutagenic action of N-methyl-N-nitrosoguanidine on propionic acid bacteria. Mikrobiologiya 42, 301–306.Google Scholar
Vorob'eva, L. I., Mashur, V. A., Baranova, N. A., Kopelevich, V. M. & Evdokimova, G. S. (1971). Enzymes of propionic acid fermentation in mutant and parent forms of Propionibacterium shermanii, Mikrobiologiya 40, 686–690.Google ScholarPubMed
Wagner, F. (1966). Vitamin B12 and related compounds. Annual Review of Biochemistry 35, 405–434.CrossRefGoogle Scholar
Wagner, F. & Bernhauer, K. (1964). New aspects of the structure of corinoid coenzymes. Annals of the New York Academy of Sciences 112, 580–589.CrossRefGoogle ScholarPubMed
Walerych, W. (1963). σ-Aminolevulinic acid dehydratese from propionic acid bacteria. Acta Biochimica Polonica 10, 243–252.Google Scholar