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.
Highlights
The transition from exponential bacterial growth into the stationary phase requires many rearrangements of gene expression to ensure survival under growth-limiting conditions
We substituted the highly conserved N-terminal arginine (R15A), which is proposed to be involved in DNA interactions [29]
Previous studies indicated that the DNA recognition and binding specificity determinants of AbrB are located primarily, or solely, within the N-terminal domains
Summary
The transition from exponential bacterial growth into the stationary phase requires many rearrangements of gene expression to ensure survival under growth-limiting conditions. AbrB is the best studied key transition state regulator of the Bacillus species and it is known to regulate more than 100 post-exponentially expressed genes, encoding for different cell functions like sporulation [1], biofilm formation [2], antibiotic production [3] or development of competence [4]. This tetrameric protein acts mainly as a repressor, only few genes are known to be activated by AbrB [5,6,7]. The high AT-content might support the inherent flexibility of the DNA to alter its conformation [16] while bound to AbrB [8,10]
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