Affiliation:
1. Department of Microbiology, Duke University Medical Center, Durham, North Carolina 27710
2. Department of Microbiology & Immunology, University of Michigan Medical School, Ann Arbor, Michigan 48104
Abstract
ABSTRACT
Specific combinations of amino acids or purine ribonucleosides and amino acids are required for efficient germination of endospores of
Bacillus anthracis
ΔSterne, a plasmidless strain, at ligand concentrations in the low-micromolar range. The amino acid
l
-alanine was the only independent germinant in
B. anthracis
and then only at concentrations of >10 mM. Inosine and
l
-alanine both play major roles as cogerminants with several other amino acids acting as efficient cogerminants (His, Pro, Trp, and Tyr combining with
l
-alanine and Ala, Cys, His, Met, Phe, Pro, Ser, Trp, Tyr, and Val combining with inosine). An ortholog to the
B. subtilis
tricistronic germination receptor operon
gerA
was located on the
B. anthracis
chromosome and named
gerS
. Disruption of
gerS
completely eliminated the ability of
B. anthracis
endospores to respond to amino-acid and inosine-dependent germination responses. The
gerS
mutation also produced a significant microlag in the aromatic-amino-acid-enhanced-alanine germination pathways. The
gerS
disruption appeared to specifically affect use of aromatic chemicals as cogerminants with alanine and inosine. We conclude that efficient germination of
B. anthracis
endospores requires multipartite signals and that
gerS
-encoded proteins act as an aromatic-responsive germination receptor.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
107 articles.
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