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Substitutional analysis of the C-terminal domain of AbrB revealed its essential role in DNA-binding activity.

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.

SUBMITTER: Neubauer S

PROVIDER: S-EPMC4022651 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Substitutional analysis of the C-terminal domain of AbrB revealed its essential role in DNA-binding activity.

Neubauer Svetlana S Dolgova Olga O Präg Gregory G Borriss Rainer R Makarewicz Oliwia O

PloS one 20140515 5

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 ...[more]

PMID: 24832089

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