scholarly journals Association of lack of cell wall teichuronic acid with formation of cell packets of Micrococcus lysodeikticus (luteus) mutants.

1975 ◽  
Vol 123 (2) ◽  
pp. 678-686 ◽  
Author(s):  
M Yamada ◽  
A Hirose ◽  
M Matsuhashi
1969 ◽  
Vol 111 (1) ◽  
pp. 1-5 ◽  
Author(s):  
D C Ellwood ◽  
D. W. Tempest

1. Quantitative determination of the anionic polymers present in the walls of Bacillus subtilis var. niger organisms undergoing transition, in a chemostat culture, from either Mg2+-limitation to PO43−-limitation or K+-limitation to PO43−-limitation showed that teichuronic acid synthesis started immediately the culture became PO43−-limited and proceeded at a rate substantially faster than the rate of biomass synthesis. 2. Simultaneously, the cell-wall teichoic acid content diminished at a rate greater than that due to dilution by newly synthesized wall material, and fragments of teichoic acid and mucopeptide accumulated in the culture extracellular fluid. 3. Equally rapid reverse changes occurred when a PO43−-limited B. subtilis var. niger culture was returned to being Mg2+-limited. 4. It is concluded that in this organism both teichoic acid and teichuronic acid syntheses are expressions of a single genotype, and a mechanism for the control of synthesis of both polymers is suggested. 5. These results are discussed with reference to the constantly changing environmental conditions that obtain in a batch culture and the variation in bacterial cell-wall composition that is reported to occur throughout the growth cycle.


1997 ◽  
Vol 272 (1) ◽  
pp. 479-485 ◽  
Author(s):  
Lingyi Deng ◽  
John S. Anderson

1969 ◽  
Vol 15 (4) ◽  
pp. 327-334
Author(s):  
M. P. Hatton

Preferential cell wall synthesis in Micrococcus lysodeikticus, as determined by an increase in the dry weight of the cell wall, took place in a medium containing DL-glutamic acid, DL-alanine, L-lysine, glycine, magnesium ions, glucose and phosphate buffer, pH 7.0. Cell wall synthesis could not be completely dissociated from protein synthesis in the 'cell wall' medium. The cell wall synthesized in the defined medium accounted for 40–56% of the total dry weight increase of the cells. Chloramphenicol had no effect on cell wall synthesis. Incorporation of uracil and guanine in the medium did not result in any increase in the amount of cell wall synthesized. DL-Glutamic acid alone, or a mixture of the three amino acids DL-alanine, L-lysine, and glycine, were capable of replacing the four amino acids present in the complete medium, but under these conditions the total dry weight of cell wall synthesized was only 75% of that produced in the complete medium. There was no reduction in cell wall synthesis when L-glutamic acid replaced DL-glutamic acid, L-alanine replaced DL-alanine, or sucrose replaced glucose in the cell wall medium. Deprivation of magnesium ions produced the greatest decrease in wall synthesis; this was the most important single factor involved in cell wall synthesis which was studied in the present investigation. There was no observable change in the chemical composition of the cell wall synthesized in the 'wall' medium when compared to that synthesized by cells grown in a complex medium.


1998 ◽  
Vol 180 (15) ◽  
pp. 4007-4010 ◽  
Author(s):  
Ying Qi ◽  
F. Marion Hulett

ABSTRACT tagA, tagD, and tuaA operons are responsible for the synthesis of cell wall anionic polymer, teichoic acid, and teichuronic acid, respectively, in Bacillus subtilis. Under phosphate starvation conditions, teichuronic acid is synthesized while teichoic acid synthesis is inhibited. Expression of these genes is controlled by PhoP-PhoR, a two-component system. It has been proposed that PhoP∼P plays a key role in the activation oftuaA and the repression of tagA andtagD. In this study, we demonstrated the role of PhoP∼P in the switch process from teichoic acid synthesis to teichuronic acid synthesis, by using an in vitro transcription system. The results indicate that PhoP∼P is sufficient to repress the transcription of the tagA and tagD promoters and also to activate the transcription of the tuaA promoter.


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