Mutants of Bacillus subtilis 168 Thermosensitive for Growth and Wall Teichoic Acid Synthesis

Microbiology ◽  
1989 ◽  
Vol 135 (5) ◽  
pp. 1325-1334 ◽  
Author(s):  
M. Briehl ◽  
H. M. Pooley ◽  
D. Karamata
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.


1998 ◽  
Vol 180 (3) ◽  
pp. 753-758 ◽  
Author(s):  
Wei Liu ◽  
Stephen Eder ◽  
F. Marion Hulett

ABSTRACT The tagAB and tagDEF operons, which are adjacent and divergently transcribed, encode genes responsible for cell wall teichoic acid synthesis in Bacillus subtilis. TheBacillus data presented here suggest that PhoP and PhoR are required for direct repression of transcription of the two operons under phosphate starvation conditions but have no regulatory role under phosphate-replete conditions. These data identify for the first time that PhoP∼P has a negative role in Pho regulon gene regulation.


1987 ◽  
Vol 207 (1) ◽  
pp. 73-81 ◽  
Author(s):  
Dimitri Karamata ◽  
Harold M. Pooley ◽  
Michel Monod

2006 ◽  
Vol 188 (23) ◽  
pp. 8313-8316 ◽  
Author(s):  
Michael A. D'Elia ◽  
Kathryn E. Millar ◽  
Terry J. Beveridge ◽  
Eric D. Brown

ABSTRACT An extensive literature has established that the synthesis of wall teichoic acid in Bacillus subtilis is essential for cell viability. Paradoxically, we have recently shown that wall teichoic acid biogenesis is dispensable in Staphylococcus aureus (M. A. D'Elia, M. P. Pereira, Y. S. Chung, W. Zhao, A. Chau, T. J. Kenney, M. C. Sulavik, T. A. Black, and E. D. Brown, J. Bacteriol. 188:4183-4189, 2006). A complex pattern of teichoic acid gene dispensability was seen in S. aureus where the first gene (tarO) was dispensable and later acting genes showed an indispensable phenotype. Here we show, for the first time, that wall teichoic acid synthesis is also dispensable in B. subtilis and that a similar gene dispensability pattern is seen where later acting enzymes display an essential phenotype, while the gene tagO, whose product catalyzes the first step in the pathway, could be deleted to yield viable mutants devoid of teichoic acid in the cell wall.


2007 ◽  
Vol 189 (19) ◽  
pp. 6816-6823 ◽  
Author(s):  
Amit P. Bhavsar ◽  
Michael A. D'Elia ◽  
Tiffany D. Sahakian ◽  
Eric D. Brown

ABSTRACT The function(s) of gram-positive wall teichoic acid is emerging with recent findings that it is an important virulence factor in the pathogen Staphylococcus aureus and that it is crucial to proper rod-shaped cell morphology of Bacillus subtilis. Despite its importance, our understanding of teichoic acid biosynthesis remains incomplete. The TagB protein has been implicated in the priming step of poly(glycerol phosphate) wall teichoic acid synthesis in B. subtilis. Work to date indicates that the TagB protein is localized to the membrane, where it adds a single glycerol phosphate residue to the nonreducing end of the undecaprenol-phosphate-linked N-acetylmannosamine-β(1,4)-N-acetylglucosamine-1-phosphate. Thus, membrane association is critical to TagB function. In this work we elucidate the mechanism of TagB membrane localization. We report the identification of a membrane targeting determinant at the amino terminus of TagB that is necessary and sufficient for membrane localization. The putative amphipathicity of this membrane targeting determinant was characterized and shown to be required for TagB function but not localization. This work shows for the first time that the amino terminus of TagB mediates membrane targeting and protein function.


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