Abstract
The global transition state regulator AbrB controls more than 100 genes of the Bacillus relatives and is known to interact with varying DNA-sequences. The DNA-binding domain of the AbrB-like proteins was proposed to be located exclusively within the amino-terminal ends. However, the recognition of DNA, and specificity of the binding mechanism, remains elusive still in view of highly differing recognition sites. Here we present a substitutional analysis to examine the role of the carboxy-terminal domain of AbrB from Bacillus subtilis and Bacillus amyloliquefaciens. Our results demonstrate that the carboxy-terminal domains of AbrB affect the DNA-binding properties of the tetrameric AbrB. Most likely, the C-termini are responsible for the cooperative character observed for AbrB interaction with some DNA targets like tycA and phyC.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacillus / genetics*
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Bacillus / metabolism
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Bacillus subtilis / genetics*
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Bacillus subtilis / metabolism
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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DNA / metabolism
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Oligonucleotides / genetics
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Peptide Synthases / metabolism
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Promoter Regions, Genetic
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Protein Binding
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Protein Structure, Tertiary
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Sequence Homology, Amino Acid
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Transcription Factors / genetics
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Transcription Factors / metabolism*
Substances
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AbrB protein, Bacillus subtilis
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Bacterial Proteins
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DNA-Binding Proteins
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Oligonucleotides
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Transcription Factors
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DNA
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Peptide Synthases
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tyrocidine synthetase
Grants and funding
This work was supported by Deutsche Forschungsgemeinschaft, DFG (grant BO 1113/9-1 to R.B.) and partially by the German Ministry for Education and Research, BMBF (grants 01EO1002 and 01Kl1204). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.