A novel teichuronic acid, the major polymer from the cell wall of Actinoplanes lobatus VKM Ac-676T

2014 ◽  
Vol 387 ◽  
pp. 19-23 ◽  
Author(s):  
Alexander S. Shashkov ◽  
Galina M. Streshinskaya ◽  
Elena M. Tul’skaya ◽  
Yulia I. Kozlova ◽  
Sof’ya N. Senchenkova ◽  
...  
Keyword(s):  
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

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.


2021 ◽  
Vol 86 (4) ◽  
pp. 506-516
Author(s):  
Alexander S. Shashkov ◽  
Elena M. Tul’skaya ◽  
Natalia V. Potekhina ◽  
Andrey S. Dmitrenok ◽  
Sofia N. Senchenkova ◽  
...  
Keyword(s):  

2002 ◽  
Vol 269 (24) ◽  
pp. 6020-6025 ◽  
Author(s):  
Alexander S. Shashkov ◽  
Larisa N. Kosmachevskaya ◽  
Galina M. Streshinskaya ◽  
Lyudmila I. Evtushenko ◽  
Olga V. Bueva ◽  
...  

2010 ◽  
Vol 2010 ◽  
pp. 1-8 ◽  
Author(s):  
Lingyi Lynn Deng ◽  
Alice A. Alexander ◽  
Sijin Lei ◽  
John S. Anderson

The cell wall teichuronic acid (TUA) ofMicrococcus luteusis a long-chain polysaccharide composed of disaccharide repeating units[-4-β-D-ManNAcAp-(1→6)α-D-Glcp−1-]n, which is covalently anchored to the peptidoglycan on the inner cell wall and extended to the outer surface of the cell envelope. An enzyme complex responsible for the TUA chain biosynthesis was purified and characterized. The 440 kDa enzyme complex, named teichuronic acid synthetase (TUAS), is an octomer composed of two kinds of glycosyltransferases, Glucosyltransferase, and ManNAcA-transferase, which is capable of catalyzing the transfer of disaccharide glycosyl residues containing both glucose and theN-acetylmannosaminuronic acid residues. TUAS displays hydrophobic properties and is found primarily associated with the cytoplasmic membrane. The purified TUAS contains carotinoids and lipids. TUAS activity is diminished by phospholipase digestion. We propose that TUAS serves as a multitasking polysaccharide assembling station on the bacterial membrane.


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