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|Title:||Promoter activation by CII, a potent transcriptional activator from bacteriophage 186|
|Citation:||Journal of Biological Chemistry, 2014; 289(46):32094-32108|
|Publisher:||American Society for Biochemistry and Molecular Biology|
|Iain Murchland, Alexandra Ahlgren-Berg, David G. Priest, Ian B. Dodd, and Keith E. Shearwin|
|Abstract:||The lysogeny promoting protein CII from bacteriophage 186 is a potent transcriptional activator, capable of mediating at least a 400-fold increase in transcription over basal activity. Despite being functionally similar to its counterpart in phage λ, it shows no homology at the level of protein sequence and does not belong to any known family of transcriptional activators. It also has the unusual property of binding DNA half-sites that are separated by 20 base pairs, center to center. Here we investigate the structural and functional properties of CII using a combination of genetics, in vitro assays, and mutational analysis. We find that 186 CII possesses two functional domains, with an independent activation epitope in each. 186 CII owes its potent activity to activation mechanisms that are dependent on both the σ⁷⁰ and α C-terminal domain (αCTD) components of RNA polymerase, contacting different functional domains. We also present evidence that like λ CII, 186 CII is proteolytically degraded in vivo, but unlike λ CII, 186 CII proteolysis results in a specific, transcriptionally inactive, degradation product with altered self-association properties.|
|Keywords:||Bacterial transcription; bacteriophage; gene transcription; promoter; proteolysis; RNA polymerase; mutational screen; protein structure-function|
|Rights:||© 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Published in the U.S.A.|
|Appears in Collections:||Molecular and Biomedical Science publications|
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