ArticleScientific reports2016
Structural and dynamics studies of a truncated variant of CI repressor from bacteriophage TP901-1.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 14 citations in OpenAlex.
- CI:Mor interactions in the lysogeny switches ofMicrobiome research reports · 2024Article
- The Complementarity of Nuclear Magnetic Resonance and Native Mass Spectrometry in Probing Protein-Protein Interactions.Advances in experimental medicine and biology · 2024Review
- Genomic analysis of a novel active prophage of Hafnia paralvei.Archives of virology · 2022Article
- Induction and Genome Analysis of HY01, a Newly Reported Prophage from an Emerging Shrimp PathogenMicroorganisms · 2021Article
- Revealing the mechanism of repressor inactivation during switching of a temperate bacteriophage.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Crystal structure of the transcriptional repressor DdrO: insight into the metalloprotease/repressor-controlled radiation response in Deinococcus.Nucleic acids research · 2019Article
- A frame-shifted gene, which rescued its function by non-natural start codons and its application in constructing synthetic gene circuits.Journal of biological engineering · 2019Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The CI repressor from the temperate bacteriophage TP901-1 consists of two folded domains, an N-terminal helix-turn-helix DNA-binding domain (NTD) and a C-terminal oligomerization domain (CTD), which we here suggest to be further divided into CTD1 and CTD2. Full-length CI is a hexameric protein, whereas a truncated version, CI∆58, forms dimers. We identify the dimerization region of CI∆58 as CTD1 and determine its secondary structure to be helical both within the context of CI∆58 and in isolation. To our knowledge this is the first time that a helical dimerization domain has been found in a phage repressor. We also precisely determine the length of the flexible linker connecting the NTD to the CTD. Using electrophoretic mobility shift assays and native mass spectrometry, we show that CI∆58 interacts with the OL operator site as one dimer bound to both half-sites, and with much higher affinity than the isolated NTD domain thus demonstrating cooperativity between the two DNA binding domains. Finally, using small angle X-ray scattering data and state-of-the-art ensemble selection techniques, we delineate the conformational space sampled by CI∆58 in solution, and we discuss the possible role that the dynamics play in CI-repressor function.
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