The quorum-sensing regulator ComA from Bacillus subtilis activates transcription using topologically distinct DNA motifs
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The quorum-sensing regulator ComA from Bacillus subtilis activates transcription using topologically distinct DNA motifs. / Wolf, Diana; Rippa, Valentina; Mobarec, Juan Carlos; Sauer, Patricia; Adlung, Lorenz; Kolb, Peter; Bischofs, Ilka B.
In: NUCLEIC ACIDS RES, Vol. 44, No. 5, 18.03.2016, p. 2160-72.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - The quorum-sensing regulator ComA from Bacillus subtilis activates transcription using topologically distinct DNA motifs
AU - Wolf, Diana
AU - Rippa, Valentina
AU - Mobarec, Juan Carlos
AU - Sauer, Patricia
AU - Adlung, Lorenz
AU - Kolb, Peter
AU - Bischofs, Ilka B
N1 - © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.
PY - 2016/3/18
Y1 - 2016/3/18
N2 - ComA-like transcription factors regulate the quorum response in numerous Gram-positive bacteria. ComA proteins belong to the tetrahelical helix-turn-helix superfamily of transcriptional activators, which bind as homodimers to inverted sequence repeats in the DNA. Here, we report that ComA from Bacillus subtilis recognizes a topologically distinct motif, in which the binding elements form a direct repeat. We provide in vitro and in vivo evidence that the canonical and non-canonical site play an important role in facilitating type I and type II promoter activation, respectively, by interacting with different subunits of RNA polymerase. We furthermore show that there is a variety of contexts in which the non-canonical site can occur and identify new direct target genes that are located within the integrative and conjugative element ICEBs1. We therefore suggest that ComA acts as a multifunctional transcriptional activator and provides a striking example for complexity in protein-DNA interactions that evolved in the context of quorum sensing.
AB - ComA-like transcription factors regulate the quorum response in numerous Gram-positive bacteria. ComA proteins belong to the tetrahelical helix-turn-helix superfamily of transcriptional activators, which bind as homodimers to inverted sequence repeats in the DNA. Here, we report that ComA from Bacillus subtilis recognizes a topologically distinct motif, in which the binding elements form a direct repeat. We provide in vitro and in vivo evidence that the canonical and non-canonical site play an important role in facilitating type I and type II promoter activation, respectively, by interacting with different subunits of RNA polymerase. We furthermore show that there is a variety of contexts in which the non-canonical site can occur and identify new direct target genes that are located within the integrative and conjugative element ICEBs1. We therefore suggest that ComA acts as a multifunctional transcriptional activator and provides a striking example for complexity in protein-DNA interactions that evolved in the context of quorum sensing.
KW - Bacillus subtilis/genetics
KW - Bacterial Proteins/genetics
KW - Base Sequence
KW - Binding Sites
KW - Cloning, Molecular
KW - DNA-Binding Proteins/genetics
KW - DNA-Directed RNA Polymerases/genetics
KW - Escherichia coli/genetics
KW - Gene Expression Regulation, Bacterial
KW - Inverted Repeat Sequences
KW - Molecular Sequence Data
KW - Nucleotide Motifs
KW - Promoter Regions, Genetic
KW - Protein Binding
KW - Protein Multimerization
KW - Protein Subunits/genetics
KW - Quorum Sensing/genetics
KW - Recombinant Proteins/genetics
KW - Transcriptional Activation
U2 - 10.1093/nar/gkv1242
DO - 10.1093/nar/gkv1242
M3 - SCORING: Journal article
C2 - 26582911
VL - 44
SP - 2160
EP - 2172
JO - NUCLEIC ACIDS RES
JF - NUCLEIC ACIDS RES
SN - 0305-1048
IS - 5
ER -