IDENTIFICATION OF TRANSCRIPTION UNITS IN THE REGION ENCOMPASSING TEICHOIC ACIDS GENES OF BACILLUS SUBTILIS

ABSTRACT Bacillus subtilis contains seven extracytoplasmic-function σ factors that activate partially overlapping regulons. We here identify four additional members of the σX regulon, pbpX (penicillin-binding protein), ywnJ, the dlt operon (d-alanylation of teichoic acids), and the pss ybfM psd operon (phosphatidylethanolamine biosynthesis). Modification of teichoic acids by esterification with d-alanine and incorporation of phosphatidylethanolamine into the cell membrane have a common consequence: in both cases positively charged amino groups are introduced into the cell envelope. The resulting reduction in the net negative charge of the cell envelope has been previously implicated as a resistance mechanism specific for cationic antimicrobial peptides. Consistent with this notion, we find that both sigX and dltA mutants are more sensitive to nisin than wild-type cells. We conclude that activation of the σX regulon serves to alter cell surface properties to provide protection against antimicrobial peptides.

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d-Alanine Substitution of Teichoic Acids as a Modulator of Protein Folding and Stability at the Cytoplasmic Membrane/Cell Wall Interface of Bacillus subtilis

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)61432-8 ◽

2000 ◽

Vol 275 (35) ◽

pp. 26696-26703 ◽

Cited By ~ 1

Author(s):

Hanne-Leena Hyyryläinen ◽

Marika Vitikainen ◽

Joanne Thwaite ◽

Hongyan Wu ◽

Matti Sarvas ◽

...

Keyword(s):

Cell Wall ◽

Protein Folding ◽

Bacillus Subtilis ◽

Cytoplasmic Membrane ◽

Alanine Substitution ◽

Teichoic Acids ◽

Membrane Cell

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The tagGH operon of Bacillus subtilis 168 encodes a two-component ABC transporter involved in the metabolism of two wall teichoic acids

Molecular Microbiology ◽

10.1111/j.1365-2958.1995.tb02306.x ◽

1995 ◽

Vol 16 (2) ◽

pp. 345-355 ◽

Cited By ~ 104

Author(s):

Vladimir Lazarevic ◽

Dimitri Karamata

Keyword(s):

Bacillus Subtilis ◽

Abc Transporter ◽

Teichoic Acids ◽

Bacillus Subtilis 168 ◽

Two Component ◽

Wall Teichoic Acids

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Phage SPP1 Reversible Adsorption to Bacillus subtilis Cell Wall Teichoic Acids Accelerates Virus Recognition of Membrane Receptor YueB

Journal of Bacteriology ◽

10.1128/jb.00349-08 ◽

2008 ◽

Vol 190 (14) ◽

pp. 4989-4996 ◽

Cited By ~ 84

Author(s):

Catarina Baptista ◽

Mário A. Santos ◽

Carlos São-José

Keyword(s):

Cell Wall ◽

Bacillus Subtilis ◽

Strong Dependence ◽

Teichoic Acid ◽

Wall Teichoic Acid ◽

Binding Interaction ◽

Host Cell Membrane ◽

Teichoic Acids ◽

Bacterial Surface ◽

Reversible Adsorption

ABSTRACT Bacteriophage SPP1 targets the host cell membrane protein YueB to irreversibly adsorb and infect Bacillus subtilis. Interestingly, SPP1 still binds to the surface of yueB mutants, although in a completely reversible way. We evaluated here the relevance of a reversible step in SPP1 adsorption and identified the receptor(s) involved. We show that reversible adsorption is impaired in B. subtilis mutants defective in the glucosylation pathway of teichoic acids or displaying a modified chemical composition of these polymers. The results indicate that glucosylated poly(glycerolphosphate) cell wall teichoic acid is the major target for SPP1 reversible binding. Interaction with this polymer is characterized by a fast adsorption rate showing low-temperature dependence, followed by a rapid establishment of an equilibrium state between adsorbed and free phages. This equilibrium is basically determined by the rate of phage dissociation, which exhibits a strong dependence on temperature compatible with an Arrhenius law. This allowed us to determine an activation energy of 22.6 kcal/mol for phage release. Finally, we show that SPP1 reversible interaction strongly accelerates irreversible binding to YueB. Our results support a model in which fast SPP1 adsorption to and desorption from teichoic acids allows SPP1 to scan the bacterial surface for rapid YueB recognition.

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