Home LiteratureArticle Details
PMID: 4404058 Published · ppublish English Journal Article

Multivalent repression of aspartic semialdehyde dehydrogenase in Escherichia coli K-12.

Journal of bacteriology ·Vol. 112 ·No. 1 ·1972-10-00 ·Pages 84-92

Boy E, Patte JC

Abstract

Mutants of Escherichia coli in which the lysine-sensitive aspartokinase is feedback-resistant are described. In these strains, as well as in the wild type, aspartic semialdehyde dehydrogenase is subject to multivalent repression by lysine, threonine, and methionine. When these amino acids were added to a culture in minimal medium, the differential rate of synthesis of the enzyme dropped to zero and remained there for about one generation.

MeSH Terms
Aspartate-Semialdehyde Dehydrogenase/antagonists & inhibitors,biosynthesis Aspartic Acid Cell-Free System Enzyme Repression/drug effects Escherichia coli/enzymology,growth & development Feedback Kinetics Lysine/pharmacology Methionine/pharmacology Mutagens Mutation Nitrosoguanidines Phosphotransferases/antagonists & inhibitors,biosynthesis Protein Biosynthesis Stereoisomerism Threonine/pharmacology Transduction, Genetic
Chemicals
Mutagens Nitrosoguanidines Threonine Aspartic Acid Methionine Aspartate-Semialdehyde Dehydrogenase Phosphotransferases Lysine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Boy E
Patte J C
References (25)
25 references, click to expand
  1. [Co-operative inhibitory effects of L-lysine with other amino acids on an aspartokinase from Escherichia coli].
    Biochim Biophys Acta. 1965 Jun 22;99(3):523-30 PMID: 5320507
  2. Regulation of protein synthesis: an alternative to the repressor-operator hypothesis.
    Proc K Ned Akad Wet C. 1965;68(4):270-6 PMID: 4221736
  3. Regulation by methionine of the synthesis of a third aspartokinase and of a second homoserine dehydrogenase in Escherichia coli K 12.
    Biochim Biophys Acta. 1967 Mar 22;136(2):245-7 PMID: 4860558
  4. Selection of Escherichia coli mutants devoid of one or of both the activities carried by a multifunctional protein.
    Biochem Biophys Res Commun. 1968 Jan 11;30(1):45-9 PMID: 4866294
  5. Translational control of gene expression.
    Cold Spring Harb Symp Quant Biol. 1966;31:321-33 PMID: 5237193
  6. Pathways of biosynthesis of aromatic amino acids and vitamins and their control in microorganisms.
    Bacteriol Rev. 1968 Dec;32(4 Pt 2):465-92 PMID: 4884716
  7. Repression of the histidine operon: effect of the first enzyme on the kinetics of repression.
    J Bacteriol. 1969 Mar;97(3):1283-90 PMID: 4887508
  8. Studies on repression of the histidine operon. II. The role of the first enzyme in control of the histidine system.
    Proc Natl Acad Sci U S A. 1969 Jun;63(2):481-8 PMID: 4895539
  9. Regulation of amino acid metabolism.
    Annu Rev Biochem. 1969;38:323-70 PMID: 4896242
  10. S-Adenosylmethionine synthetase deficient mutants of Escherichia coli K-12 with impaired control of methionine biosynthesis.
    Biochem Biophys Res Commun. 1970 Mar 27;38(6):1120-6 PMID: 4908544
  11. Tryptophan messenger translation in Escherichia coli.
    J Mol Biol. 1970 Jul 28;51(2):435-47 PMID: 4922205
  12. Regulation at the level of translation in the arginine pathway of Escherichia coli K12.
    J Mol Biol. 1970 Jul 28;51(2):449-51 PMID: 4922206
  13. Regulation of S-adenosylmethionine synthetase in Escherichia coli.
    J Bacteriol. 1970 Nov;104(2):734-47 PMID: 4923071
  14. Translational repression in the arginine system of Escherichia coli.
    Proc Natl Acad Sci U S A. 1970 Dec;67(4):1703-9 PMID: 4923118
  15. Regulation of the lysine biosynthetic pathway of Escherichia coli K12. Isolation, molecular weight and amino acid analysis of the lysine sensitive aspartokinase.
    Eur J Biochem. 1970 Jul;15(1):111-5 PMID: 4923154
  16. Two mutations in the first gene of the histidine operon of Salmonella typhimurium affecting control.
    J Bacteriol. 1971 Apr;106(1):227-37 PMID: 4928009
  17. Involvement of threonine deaminase in multivalent repression of the isoleucine-valine pathway in Saccharomyces cerevisiae.
    Proc Natl Acad Sci U S A. 1971 Sep;68(9):2169-72 PMID: 4943789
  18. Biosynthetic interrelations of lysine, diaminopimelic acid, and threonine in mutants of Escherichia coli.
    Nature. 1952 Mar 29;169(4300):534-6 PMID: 14929228
  19. The preparation of S-adenosylmethionine.
    J Biol Chem. 1957 Dec;229(2):1051-7 PMID: 13502364
  20. Genetic regulatory mechanisms in the synthesis of proteins.
    J Mol Biol. 1961 Jun;3:318-56 PMID: 13718526
  21. The branching point in diaminopimelic acid synthesis.
    J Biol Chem. 1962 Feb;237:482-4 PMID: 13898711
  22. [Retro-inhibition and repression of the homoserine dehydrogenase of Escherichia coli].
    Biochim Biophys Acta. 1963 Jan 8;67:16-30 PMID: 13941895
  23. Control of isoleucine, valine, and leucine biosynthesis. I. Multivalent repression.
    Proc Natl Acad Sci U S A. 1962 Oct 15;48:1804-8 PMID: 13959618
  24. [Coordinated derepression of lysine-aspartokinase and of semi-aspartaldehyde dehydrogenase in Escherichia coli].
    C R Hebd Seances Acad Sci. 1963 Mar 25;256:2939-41 PMID: 14022037
  25. Transduction of lysogeny in Escherichia coli.
    Virology. 1955 Jul;1(2):207-20 PMID: 13267988
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.112.1.84-92.1972
Published
1972-10-00
Pages
84-92
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC251383
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.112.1.84-92.1972 PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2