Skip to main content
Log in

Regulation of biosynthesis of aspartate family amino acids in the photosynthetic bacterium Rhodopseudomonas palustris

  • Published:
Archives of Microbiology Aims and scope Submit manuscript

Abstract

The four amino acids of the “aspartate family” (l-lysine, l-methionine, l-threonine, and l-isoleucine) are produced in bacteria by a branched biosynthetic pathway. Regulation of synthesis of early common intermediates and of carbon flow through distal branches of the pathway requires operation of a number of subtle feedback controls, which are integrated so as to ensure “balanced” synthesis of the several end products. Earlier studies with nonsulfur purple photosynthetic bacteria were instrumental in revealing the existence of alternative regulatory schemes, and in this communication we report on the control pattern of a representative of this physiological group not previously investigated, Rhodopseudomonas palustris. The results obtained from study of the properties of four “key” regulatory enzymes of the aspartate family pathway (β-aspartokinase, homoserine dehydrogenase, homoserine kinase, and threonine deaminase) and of the effects of exogenous amino acids (i. e., the end products) on growth of the bacterium indicate that the control schema in Rps. palustris differs substantially from the schemes described for other Rhodopseudomonas species, but resembles the regulatory pattern observed in Rhodospirillum rubrum.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

A:

absorbancy

AK:

β-aspartokinase

ASA:

aspartate β-semialdehyde

DTT:

dithiothreitol

HS:

l-homoserine

HSDH:

homoserine dehydrogenase

HSK:

homoserine kinase

I:

l-isoleucine

KU:

Klett-Summerson photometer units

L:

l-lysine

M:

l-isoleucine

KU:

Klett-Summerson photometer units

L:

l-lysine

M:

l-methionine

ME:

β-mercaptoethanol

PABA:

p-aminobenzoic acid

T:

l-threonine

TD:

threonine deaminase

RCV:

synthetic growth medium (see text)

YP agar:

medium containing 0.3% yeast extract, 0.3% peptone, and 1.5% agar

Y2T:

synthetic growth medium (see text)

References

  • Andrews, P.: The gel-filtration behaviour of proteins related to their molecular weight over a wide range. Biochem. J. 98, 595–606 (1965)

    Google Scholar 

  • Baumann, L., Baumann, P.: Regulation of aspartokinase activity in nonfermentative, marine eubacteria. Arch. Microbiol. 95, 1–18 (1974)

    Google Scholar 

  • Black, S.: β-aspartyl phosphate and aspartic-β-semialdehyde. In: S. P. Colowick, N. O. Kaplan, Eds., Methods in enzymology, Vol. 6, pp. 622–624. New York: Academic Press 1962

    Google Scholar 

  • Black, S., Wright, N. G.: β-aspartokinase and β-aspartyl phosphate. J. biol. Chem. 213, 27–38 (1955)

    Google Scholar 

  • Burlant, L., Datta, P., Gest, H.: Control of enzyme activity in growing bacterial cells by concerted feedback inhibition. Science 148, 1351–1353 (1965)

    Google Scholar 

  • Cohen, G. N., Stanier, R. Y., LeBras, G.: Regulation of the biosynthesis of amino acids of the aspartate family in coliform bacteria and pseudomonads. J. Bact. 99, 791–801 (1969)

    Google Scholar 

  • Datta, P.: Regulation of branched biosynthetic pathways in bacteria. Science 165, 556–562 (1969)

    Google Scholar 

  • Datta, P., Dungan, S. M., Feldberg, R. S.: Regulation of amino acid biosynthesis of the aspartate pathway in different microorganisms. In: Z. Vanek, Z. Hostalek, J. Cudlin, Eds., Genetics of industrial microorganisms, Vol. 1, pp. 177–191. Prague: Academia, Publishing House of the Czechoslovak Acad. Sci. 1973

    Google Scholar 

  • Datta, P., Gest, H.: Alternative patterns of end product control in biosynthesis of amino acids of the aspartic family. Nature (Lond.) 203, 1259–1261 (1964a)

    Google Scholar 

  • Datta, P., Gest, H.: Control of enzyme activity by concerted feedback inhibition. Proc. nat. Acad. Sci. (Wash.) 52, 1004–1009 (1964b)

    Google Scholar 

  • Datta, P., Gest, H.: Homoserine dehydrogenase of Rhodospirillum rubrum. Purification, properties and feedback control of activity. J. biol. Chem. 240, 3023–3033 (1965)

    Google Scholar 

  • Dungan, S. M., Datta, P.: Concerted feedback inhibition. Purification and some properties of aspartokinase from Pseudomonas fluorescens. J. biol. Chem. 248, 8534–8540 (1973)

    Google Scholar 

  • Friedemann, T. E., Haugen, G. E.: Pyruvic acid. II. The determination of keto acids in blood and urine. J. biol. Chem. 147, 415–442 (1943)

    Google Scholar 

  • Gibson, K. D., Neuberger, A., Tait, G. H.: Studies on the biosynthesis of porphyrin and bacteriochlorophyll by Rhodopseudomonas spheroides. 2. The effects of ethionine and threonine. Biochem. J. 83, 550–559 (1962)

    Google Scholar 

  • Greenberg, D. M.: Cystathionine and homoserine cleavage. In: S. P. Colowick, N. O. Kaplan, Eds., Methods in enzymology, Vol. 5, pp. 936–947. New York: Academic Press 1962

    Google Scholar 

  • Guirard, B. M., Ames, B., Snell, E. E.: Salmonella typhimurium mutants with alternate requirements for vitamin B6 or isoleucine. J. Bact. 108, 359–363 (1971)

    Google Scholar 

  • Hatfield, G. M., Umbarger, H. E.: Threonine deaminase from Bacillus subtilis. I. Purification of the enzyme. J. biol. Chem. 245, 1736–1741 (1970)

    Google Scholar 

  • Hughes, M., Brenneman, C., Gest, H.: Feedback sensitivity of threonine deaminase in two species of photosynthetic bacteria. J. Bact. 88, 1201–1202 (1964)

    Google Scholar 

  • Lowry, O. H., Rosebrough, N. J., Farr, A. L., Randall, R. J.: Protein measurement with the Folin phenol reagent. J. biol. Chem. 193, 265–275 (1951)

    Google Scholar 

  • Matsuo, Y., Greenberg, D. M.: A crystalline enzyme that cleaves homoserine and cystathionine. I. Isolation procedures and some physicochemical properties. J. biol. Chem. 230, 545–560 (1958)

    Google Scholar 

  • Moore, S., Stein, W. H.: A modified ninhydrin reagent for the photometric determination of amino acids and related compounds. J. biol. Chem. 211, 907–913 (1954)

    Google Scholar 

  • van Niel, C. B.: The culture, general physiology, morphology, and classification of non-sulfur purple and brown bacteria. Bact. Rev. 8, 1–118 (1944)

    Google Scholar 

  • Ning, C., Gest, H.: Regulation of l-isoleucine biosynthesis in the photosynthetic bacterium Rhodospirillum rubrum. Proc. nat. Acad. Sci. (Wash.) 56, 1823–1827 (1966)

    Google Scholar 

  • Paulus, H., Gray, E.: Multivalent feedback inhibition of aspartokinase in Bacillus polymyxa. J. biol. Chem. 239, 4008–4009 (1964)

    Google Scholar 

  • Robert-Gero, M., LeBorgne, L., Cohen, G. N.: Concerted feedback inhibition of the aspartokinase of Rhodospirillum tenue by threonine and methionine: a novel pattern. J. Bact. 112, 251–258 (1972)

    Google Scholar 

  • Schildkraut, I., Greer, S.: Threonine synthetase-catalyzed conversion of phosphohomoserine to α-ketobutyrate in Bacillus subtilis. J. Bact. 115, 777–785 (1973)

    Google Scholar 

  • Stadtman, E. R.: Symposium on multiple forms of enzymes and control mechanisms. II. Enzyme multiplicity and function in the regulation of divergent metabolic pathways. Bact. Rev. 27, 170–180 (1963)

    Google Scholar 

  • Stadtman, E. R., Cohen, G. N., LeBras, G., de Robichon-Szulmajster, H.: Feedback inhibition and repression of aspartokinase activity in Escherichia coli and Saccharomyces cerevisiae. J. biol. Chem. 236, 2033–2038 (1961)

    Google Scholar 

  • Sturani, E., Datta, P., Hughes, M., Gest, H.: Regulation of enzyme activity by specific reversal of feedback inhibition. Science 141, 1053–1054 (1963)

    Google Scholar 

  • Theze, J., Kleidman, L., Saint Girons, I.: Homoserine kinase from Escherichia coli K-12: properties, inhibition by l-threonine, and regulation of biosynthesis. J. Bact. 118, 577–581 (1974)

    Google Scholar 

  • Umbarger, H. E.: Threonine deaminase. Adv. Enzymol. 37, 347–395 (1973)

    Google Scholar 

  • Umbarger, H. E., Brown, B.: Threonine deaminase in Escherichia coli. II. Evidence for two l-threonine deaminases. J. Bact. 73, 105–112 (1957)

    Google Scholar 

  • Wormser, E. H., Pardee, A. B.: Regulation of threonine biosynthesis in Escherichia coli. Arch. Biochem. 78, 416–432 (1948)

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Yen, Hc., Gest, H. Regulation of biosynthesis of aspartate family amino acids in the photosynthetic bacterium Rhodopseudomonas palustris . Arch. Microbiol. 101, 187–210 (1974). https://doi.org/10.1007/BF00455938

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00455938

Key words

Navigation