Changes in Cell Dimensions During Amino Acid Starvation of Escherichia Coli

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1982 Oct 1

PMID 6749809

Citations 17

Authors

N Grossman

E Z Ron

C L Woldringh

Affiliations

Soon will be listed here.

Abstract

Electron microscopic analysis was used to study cells of Escherichia coli B and K-12 during and after amino acid starvation. The results confirmed our previous conclusion that cell division and initiation of DNA replication occur at a smaller cell volume after amino acid starvation. Although during short starvation periods, the number of constricting cells decreased due to residual division, it appears that during prolonged starvation, cells of E. coli B and K-12 were capable of initiating new constrictions. During amino acid starvation, cell diameter decreased significantly. The decrease was reversed only after two generation times after the resumption of protein synthesis and was larger in magnitude than that previously observed before division (F. J. Trueba and C. L. Woldringh, J. Bacteriol. 142:869-878, 1980). This decrease in cell diameter correlates with synchronization of cell division which has been shown to occur after amino acid starvation.

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References

Schlesinger S . Inhibition of growth of Escherichia coli and of homoserine O-transsuccinylase by alpha-methylmethionine. J Bacteriol. 1967; 94(2):327-32. PMC: 315044. DOI: 10.1128/jb.94.2.327-332.1967. View

Moyed H . False feedback inhibition: inhibition of tryptophan biosynthesis by 5-methyltryptophan. J Biol Chem. 1960; 235:1098-102. View

Zaritsky A, Pritchard R . Changes in cell size and shape associated with changes in the replication time of the chromosome of Escherichia coli. J Bacteriol. 1973; 114(2):824-37. PMC: 251845. DOI: 10.1128/jb.114.2.824-837.1973. View

Jones N, DONACHIE W . Chromosome replication, transcription and control of cell division in Escherichia coli. Nat New Biol. 1973; 243(125):100-3. View

Ron E, Rozenhak S, Grossman N . Synchronization of cell division in Escherichia coli by amino acid starvation: strain specificity. J Bacteriol. 1975; 123(1):374-6. PMC: 235729. DOI: 10.1128/jb.123.1.374-376.1975. View

Ishiguro E, Ramey W . Stringent control of peptidoglycan biosynthesis in Escherichia coli K-12. J Bacteriol. 1976; 127(3):1119-26. PMC: 232902. DOI: 10.1128/jb.127.3.1119-1126.1976. View

GOLDBERG A, St John A . Intracellular protein degradation in mammalian and bacterial cells: Part 2. Annu Rev Biochem. 1976; 45:747-803. DOI: 10.1146/annurev.bi.45.070176.003531. View

Ron E, Grossman N, Helmstetter C . Control of cell division in Escherichia coli: effect of amino acid starvation. J Bacteriol. 1977; 129(2):569-73. PMC: 234977. DOI: 10.1128/jb.129.2.569-573.1977. View

Woldringh C, de Jong M, van den Berg W, Koppes L . Morphological analysis of the division cycle of two Escherichia coli substrains during slow growth. J Bacteriol. 1977; 131(1):270-9. PMC: 235419. DOI: 10.1128/jb.131.1.270-279.1977. View

10.

Ishiguro E, Ramey W . Involvement of the relA gene product and feedback inhibition in the regulation of DUP-N-acetylmuramyl-peptide synthesis in Escherichia coli. J Bacteriol. 1978; 135(3):766-74. PMC: 222446. DOI: 10.1128/jb.135.3.766-774.1978. View

11.

Trueba F, Woldringh C . Changes in cell diameter during the division cycle of Escherichia coli. J Bacteriol. 1980; 142(3):869-78. PMC: 294112. DOI: 10.1128/jb.142.3.869-878.1980. View

12.

Grossman N, Ron E . Initiation of deoxyribonucleic acid replication in Escherichia coli B: uncoupling from mass/deoxyribonucleic acid ratio. J Bacteriol. 1980; 143(1):100-4. PMC: 294188. DOI: 10.1128/jb.143.1.100-104.1980. View

13.

Dwek R, Kobrin L, Grossman N, Ron E . Synchronization of cell division in microorganisms by percoll gradients. J Bacteriol. 1980; 144(1):17-21. PMC: 294577. DOI: 10.1128/jb.144.1.17-21.1980. View

14.

Umbarger H, Brown B . Isoleucine and valine metabolism in Escherichia coli. V. Antagonism between isoleucine and valine. J Bacteriol. 1955; 70(2):241-8. PMC: 357668. DOI: 10.1128/jb.70.2.241-248.1955. View

15.

Schaechter M, MAALOE O, KJELDGAARD N . Dependency on medium and temperature of cell size and chemical composition during balanced grown of Salmonella typhimurium. J Gen Microbiol. 1958; 19(3):592-606. DOI: 10.1099/00221287-19-3-592. View

16.

Wolf B, Newman A, Glaser D . On the origin and direction of replication of the Escherichia coli K12 chromosome. J Mol Biol. 1968; 32(3):611-29. DOI: 10.1016/0022-2836(68)90346-x. View