<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>9(5)</volume><submitter>Neubauer S</submitter><pubmed_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.</pubmed_abstract><journal>PloS one</journal><pagination>e97254</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC4022651</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Substitutional analysis of the C-terminal domain of AbrB revealed its essential role in DNA-binding activity.</pubmed_title><pmcid>PMC4022651</pmcid><pubmed_authors>Dolgova O</pubmed_authors><pubmed_authors>Prag G</pubmed_authors><pubmed_authors>Neubauer S</pubmed_authors><pubmed_authors>Makarewicz O</pubmed_authors><pubmed_authors>Borriss R</pubmed_authors></additional><is_claimable>false</is_claimable><name>Substitutional analysis of the C-terminal domain of AbrB revealed its essential role in DNA-binding activity.</name><description>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.</description><dates><release>2014-01-01T00:00:00Z</release><publication>2014</publication><modification>2021-03-03T08:49:22Z</modification><creation>2019-03-26T23:24:49Z</creation></dates><accession>S-EPMC4022651</accession><cross_references><pubmed>24832089</pubmed><doi>10.1371/journal.pone.0097254</doi></cross_references></HashMap>