Teichoic acids as components of a specific phage receptor in Bacillus subtilis

ABSTRACTConjugation activity of plasmid pLS20 fromBacillus subtilissubsp.nattois induced when cells are diluted into fresh medium and diminishes as cells enter into stationary-phase growth. Transcriptional profiling shows that during mid-exponential growth, more than 5% of the host genes are affected in the presence of the plasmid, in contrast to the minor changes seen in freshly diluted and stationary-phase cells. Changes occurred in many metabolic pathways, although pLS20 does not confer any detectable burden on its host cell, as well as in membrane and cell wall-associated processes, in the large motility operon, and in several other cellular processes. In agreement with these changes, we found considerable alterations in motility and enzyme activity and increased resistance against several different forms of stress in cells containing the plasmid, revealing that the presence of pLS20 has a broad impact on the physiology of its host cell and increases its stress resistance in multiple aspects. Additionally, we found that the lack of chromosomal geneyueB, known to encode a phage receptor protein, which is upregulated in cells containing pLS20, strongly reduced conjugation efficiency, revealing that pLS20 not only increases fitness of its host but also employs host proteins for efficient transfer into a new cell.

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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 ◽

10.1074/jbc.m003804200 ◽

2000 ◽

Cited By ~ 29

Author(s):

H.-L. Hyyrylainen

Keyword(s):

Cell Wall ◽

Protein Folding ◽

Bacillus Subtilis ◽

Cytoplasmic Membrane ◽

Alanine Substitution ◽

Teichoic Acids ◽

Membrane Cell

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Antibiotic sensitivity reveals that wall teichoic acids mediate DNA binding during competence in Bacillus subtilis

Nature Communications ◽

10.1038/s41467-018-07553-8 ◽

2018 ◽

Vol 9 (1) ◽

Cited By ~ 4

Author(s):

Nicolas Mirouze ◽

Cécile Ferret ◽

Charlène Cornilleau ◽

Rut Carballido-López

Keyword(s):

Bacillus Subtilis ◽

Dna Binding ◽

Antibiotic Sensitivity ◽

Teichoic Acids ◽

Wall Teichoic Acids

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Structure and functions of linkage unit intermediates in the biosynthesis of ribitol teichoic acids in Staphylococcus aureus H and Bacillus subtilis W23

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1986.tb10469.x ◽

1986 ◽

Vol 161 (2) ◽

pp. 479-489 ◽

Cited By ~ 36

Author(s):

Kohei YOKOYAMA ◽

Tomoyuki MIYASHITA ◽

Yoshio ARAKI ◽

Eiji ITO

Keyword(s):

Staphylococcus Aureus ◽

Bacillus Subtilis ◽

Teichoic Acids ◽

Structure And Functions

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The Bacillus subtilis Extracytoplasmic-Function σX Factor Regulates Modification of the Cell Envelope and Resistance to Cationic Antimicrobial Peptides

Journal of Bacteriology ◽

10.1128/jb.186.4.1136-1146.2004 ◽

2004 ◽

Vol 186 (4) ◽

pp. 1136-1146 ◽

Cited By ~ 111

Author(s):

Min Cao ◽

John D. Helmann

Keyword(s):

Bacillus Subtilis ◽

Antimicrobial Peptides ◽

Cell Envelope ◽

Resistance Mechanism ◽

Penicillin Binding Protein ◽

Wild Type ◽

Amino Groups ◽

Cationic Antimicrobial Peptides ◽

Teichoic Acids ◽

Positively Charged

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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