ArticleJournal of bacteriology2010
Characterization of the CI repressor protein encoded by the temperate lactococcal phage TP901-1.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- CRISPRi-mediated repression of threeJournal of bacteriology · 2025Article
- Directed evolution of bacteriophages: thwarted by prolific prophage.Applied and environmental microbiology · 2024Article
- 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
- Repression of the lysogenic PScientific reports · 2020Article
- Bacterial and Archaeal Viruses of Himalayan Hot Springs at Manikaran Modulate Host Genomes.Frontiers in microbiology · 2018Article
- Structural and dynamics studies of a truncated variant of CI repressor from bacteriophage TP901-1.Scientific reports · 2016Article
- Clear Plaque Mutants of Lactococcal Phage TP901-1.PloS one · 2016Article
- A super-family of transcriptional activators regulates bacteriophage packaging and lysis in Gram-positive bacteria.Nucleic acids research · 2013Article
- Key players in the genetic switch of bacteriophage TP901-1.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The gene regulatory mechanism determining the developmental pathway of the temperate bacteriophage TP901-1 is regulated by two phage-encoded proteins, CI and MOR. Functional domains of the CI repressor were investigated by introducing linkers of 15 bp at various positions in cI and by limited proteolysis of purified CI protein. We show that insertions of five amino acids at positions in the N-terminal half of CI resulted in mutant proteins that could no longer repress transcription from the lytic promoter, P(L). We confirmed that the N-terminal domain of CI contains the DNA binding site, and we showed that this part of the protein is tightly folded, whereas the central part and the C-terminal part of CI seem to contain more flexible structures. Furthermore, insertions at several different positions in the central part of the CI protein reduced the cooperative binding of CI to the operator sites and possibly altered the interaction with MOR.
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