The peptide XIP induces competence in Streptococcus
sobrinus. (A) The ComRS competence
pathway in Streptococcus mutans forms an
autocrine signaling loop. An unknown protein cleaves the leader
peptide from ComS and exports the XIP precursor. Activated XIP
is imported, where it facilitates dimerization of the
transcriptional regulator ComR. The ComR/XIP complex binds a DNA
motif to promote transcription of comX and
comS. (B) The ComR/XIP
binding motif appears upstream of the sigma factor
comX. Using this sequence, we identified
a comS gene in 2 strains of S.
sobrinus. The comS gene appears
downstream of a homolog of the regulator comR.
(C) S. sobrinus strains NIDR
6715-7 and NCTC 10919 can be transformed with exogenous XIP.
Both strains were transformed with a plasmid expressing LacZ.
When plated with X-gal, the plasmid-carrying strains produce a
blue color, but the wild type strains do not. (D)
The transformation efficiency of S. sobrinus
strain NCTC 10919 increases with XIP concentration.
Transformation assays used linear DNA with homology to regions
flanking comR. No transformants were observed
without XIP. (E) Transformation efficiency peaks in
the midexponential phase. Transformation assays were performed
with strain NCTC 10919 and the pLacZ plasmid (Appendix Fig. 1) by using the predicted XIP
for strains SL1 (LMCTIVR) and NIDR 6715-7 (LMCTIAR). No XIP
precursor gene (comS) is found in the NCTC
10919 genome. (F) The S. sobrinus
ComS peptides differ from sequences in S. mutans,
Streptococcus salivarius, and
Streptococcus thermophilus. In
particular, all previously known XIP sequences in streptococci
contain 2 aromatic amino acids; the XIP in S.
sobrinus has none.