Development and Characterization of a Xylose-Dependent System for Expression of Cloned Genes in Bacillus subtilis: Conditional Complementation of a Teichoic Acid Mutant

ABSTRACT The Bacillus subtilis thermosensitive mutant ts-21 bears two C-G→T-A transitions in the mnaA gene. At the nonpermissive temperature it is characterized by coccoid cell morphology and reduced cell wall phosphate content. MnaA converts UDP-N-acetylglucosamine into UDP-N-acetylmannosamine, a precursor of the teichoic acid linkage unit.

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Genetic and biochemical characterization of Bacillus subtilis 168 mutants specifically blocked in the synthesis of the teichoic acid poly(3-O- -D-glucopyranosyl-N-acetylgalactosamine 1-phosphate): gneA, a new locus, is associated with UDP-N-acetylglucosamine 4-epimerase activity

Journal of General Microbiology ◽

10.1099/00221287-137-4-943 ◽

1991 ◽

Vol 137 (4) ◽

pp. 943-950 ◽

Cited By ~ 35

Author(s):

A.-I. Estrela ◽

H. M. Pooley ◽

H. de Lencastre ◽

D. Karamata

Keyword(s):

Bacillus Subtilis ◽

Biochemical Characterization ◽

Teichoic Acid ◽

Bacillus Subtilis 168

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GtcA is required for LTA glycosylation in Listeria monocytogenes serovar 1/2a and Bacillus subtilis

10.1101/2019.12.12.873851 ◽

2019 ◽

Cited By ~ 2

Author(s):

Jeanine Rismondo ◽

Talal F. M. Haddad ◽

Yang Shen ◽

Martin J. Loessner ◽

Angelika Gründling

Keyword(s):

Cell Wall ◽

Bacillus Subtilis ◽

Listeria Monocytogenes ◽

Teichoic Acid ◽

Lipoteichoic Acid ◽

Wall Teichoic Acid ◽

Gram Positive Bacteria ◽

Cell Wall Polymers ◽

Galactose Residue

ABSTRACTThe cell wall polymers wall teichoic acid (WTA) and lipoteichoic acid (LTA) are often modified with glycosyl and D-alanine residues. Recent studies have shown that a three-component glycosylation system is used for the modification of LTA in several Gram-positive bacteria including Bacillus subtilis and Listeria monocytogenes. In the L. monocytogenes 1/2a strain 10403S, the cytoplasmic glycosyltransferase GtlA is thought to use UDP-galactose to produce the C55-P-galactose lipid intermediate, which is transported across the membrane by an unknown flippase. Next, the galactose residue is transferred onto the LTA backbone on the outside of the cell by the glycosyltransferase GtlB. Here we show that GtcA is necessary for the glycosylation of LTA in L. monocytogenes 10403S and B. subtilis 168 and we hypothesize that these proteins act as C55-P-sugar flippases. With this we revealed that GtcA is involved in the glycosylation of both teichoic acid polymers in L. monocytogenes 10403S, namely WTA with N-acetylglucosamine and LTA with galactose residues. These findings indicate that the L. monocytogenes GtcA protein can act on different C55-P-sugar intermediates. Further characterization of GtcA in L. monocytogenes led to the identification of residues essential for its overall function as well as residues, which predominately impact WTA or LTA glycosylation.GRAPHICAL ABSTRACT

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The N-Acetylmannosamine Transferase Catalyzes the First Committed Step of Teichoic Acid Assembly in Bacillus subtilis and Staphylococcus aureus

Journal of Bacteriology ◽

10.1128/jb.00611-08 ◽

2009 ◽

Vol 191 (12) ◽

pp. 4030-4034 ◽

Cited By ~ 48

Author(s):

Michael A. D'Elia ◽

James A. Henderson ◽

Terry J. Beveridge ◽

David E. Heinrichs ◽

Eric D. Brown

Keyword(s):

Staphylococcus Aureus ◽

Bacillus Subtilis ◽

Teichoic Acid ◽

Acid Synthesis ◽

Early Gene ◽

Wall Teichoic Acid ◽

And Staphylococcus Aureus ◽

Made In

ABSTRACT There have been considerable strides made in the characterization of the dispensability of teichoic acid biosynthesis genes in recent years. A notable omission thus far has been an early gene in teichoic acid synthesis encoding the N-acetylmannosamine transferase (tagA in Bacillus subtilis; tarA in Staphylococcus aureus), which adds N-acetylmannosamine to complete the synthesis of undecaprenol pyrophosphate-linked disaccharide. Here, we show that the N-acetylmannosamine transferases are dispensable for growth in vitro, making this biosynthetic enzyme the last dispensable gene in the pathway, suggesting that tagA (or tarA) encodes the first committed step in wall teichoic acid synthesis.

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