Repression of the lysogenic P
Bacteriophages
/ genetics
Binding Sites
/ genetics
DNA, Viral
/ genetics
DNA-Binding Proteins
/ genetics
Enterococcus
/ virology
Gene Expression Regulation, Viral
/ genetics
Genome, Viral
/ genetics
Lactococcus lactis
/ genetics
Lysogeny
/ genetics
Operator Regions, Genetic
/ genetics
Promoter Regions, Genetic
/ genetics
Regulatory Elements, Transcriptional
/ genetics
Repressor Proteins
/ genetics
Staphylococcus
/ virology
Streptococcus
/ virology
Trans-Activators
/ genetics
Viral Regulatory and Accessory Proteins
/ genetics
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
26 05 2020
26 05 2020
Historique:
received:
31
10
2019
accepted:
04
05
2020
entrez:
28
5
2020
pubmed:
28
5
2020
medline:
15
12
2020
Statut:
epublish
Résumé
A functional genetic switch from the lactococcal bacteriophage TP901-1, deciding which of two divergently transcribing promoters becomes most active and allows this bi-stable decision to be inherited in future generations requires a DNA region of less than 1 kb. The fragment encodes two repressors, CI and MOR, transcribed from the P
Identifiants
pubmed: 32457340
doi: 10.1038/s41598-020-65493-0
pii: 10.1038/s41598-020-65493-0
pmc: PMC7250872
doi:
Substances chimiques
DNA, Viral
0
DNA-Binding Proteins
0
Repressor Proteins
0
Trans-Activators
0
Viral Regulatory and Accessory Proteins
0
phage repressor proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8659Références
Oppenheim, A. B., Kobiler, O., Stavans, J., Court, D. L. & Adhya, S. Switches in Bacteriophage Lambda Development. Annu. Rev. Genet. 39, 409–429 (2005).
doi: 10.1146/annurev.genet.39.073003.113656
pubmed: 16285866
Madsen, P. L., Johansen, A. H., Hammer, K. & Brøndsted, L. The genetic switch regulating activity of early promoters of the temperate lactococcal bacteriophage TP901-1. J. Bacteriol. 181, 7430–7438 (1999).
doi: 10.1128/JB.181.24.7430-7438.1999
pubmed: 10601198
pmcid: 94198
Pedersen, M. & Hammer, K. The Role of MOR and the CI Operator Sites on the Genetic Switch of the Temperate Bacteriophage TP901-1. J. Mol. Biol. 384, 577–589 (2008).
doi: 10.1016/j.jmb.2008.09.071
pubmed: 18930065
Alsing, A., Pedersen, M., Sneppen, K. & Hammer, K. Key players in the genetic switch of bacteriophage TP901-1. Biophys. J. 100, 313–321 (2011).
doi: 10.1016/j.bpj.2010.12.3681
pubmed: 21244827
pmcid: 3021656
Rasmussen, K. K. et al. Structural and dynamics studies of a truncated variant of CI repressor from bacteriophage TP901-1. Sci. Rep. 6, (2016).
Breüner, A., Brøndsted, L. & Hammer, K. Novel organization of genes involved in prophage excision identified in the temperate lactococcal bacteriophage TP901-1. J. Bacteriol. 181, 7291–7297 (1999).
doi: 10.1128/JB.181.23.7291-7297.1999
pubmed: 10572133
pmcid: 103692
Kenny, J. G. et al. Characterization of the lytic-lysogenic switch of the lactococcal bacteriophage Tuc2009. Virology 347, 434–446 (2006).
doi: 10.1016/j.virol.2005.11.041
pubmed: 16410016
Frandsen, K. H. et al. Binding of the N-terminal domain of the lactococcal bacteriophage tp901-1 ci repressor to its target DNA: A crystallography, small angle scattering, and nuclear magnetic resonance study. Biochemistry 52, 6892–6904 (2013).
doi: 10.1021/bi400439y
pubmed: 24047404
Rasmussen, K. K. et al. Structural basis of the bacteriophage TP901-1 CI repressor dimerization and interaction with DNA. FEBS Letters https://doi.org/10.1002/1873-3468.13060 (2018).
doi: 10.1002/1873-3468.13060
pubmed: 29683476
Pedersen, M., Kilstrup, M. & Hammer, K. Identification of DNA-binding sites for the activator involved in late transcription of the temperate lactococcal phage TP901-1. Virology 345, 446–456 (2006).
doi: 10.1016/j.virol.2005.10.007
pubmed: 16297953
Nakanishi, H., Pedersen, M., Alsing, A. K. & Sneppen, K. Modeling of the Genetic Switch of Bacteriophage TP901-1: A Heteromer of CI and MOR Ensures Robust Bistability. J. Mol. Biol. 394, 15–28 (2009).
doi: 10.1016/j.jmb.2009.08.075
pubmed: 19747486
Graña, D., Gardella, T. & Susskind, M. M. The effects of mutations in the ant promoter of phage P22 depend on context. Genetics 120, 319–327 (1988).
pubmed: 3143618
pmcid: 1203512
Shearwin, K. E., Brumby, A. M. & Egan, J. B. The tum protein of coliphage 186 is an antirepressor. J. Biol. Chem. 273, 5708–5715 (1998).
doi: 10.1074/jbc.273.10.5708
pubmed: 9488703
Brumby, A. M., Lamont, I., Dodd, I. B. & Egan, J. B. Defining the SOS operon of coliphage 186. Virology 219, 105–114 (1996).
doi: 10.1006/viro.1996.0227
pubmed: 8623519
Velleman, M., Heinzel, T. & Schuster, H. The Bof protein of bacteriophage P1 exerts its modulating function by formation of a ternary complex with operator DNA and C1 repressor. J. Biol. Chem. 267, 12174–12181 (1992).
pubmed: 1601883
Schaefer, T. S. & Hays, J. B. The bof gene of bacteriophage P1: DNA sequence and evidence for roles in regulation of phage c1 and ref genes. J. Bacteriol. 172, 3269–3277 (1990).
doi: 10.1128/JB.172.6.3269-3277.1990
pubmed: 2345146
pmcid: 209135
Heinrich, J., Velleman, M. & Schuster, H. The tripartite immunity system of phages P1 and P7. FEMS Microbiol. Rev. 17, 121–126 (1995).
doi: 10.1111/j.1574-6976.1995.tb00193.x
pubmed: 7669337
Yu, A. & Haggard-Ljungquist, E. The Cox protein is a modulator of directionality in bacteriophage P2 site- specific recombination. J. Bacteriol. 175, 7848–7855 (1993).
doi: 10.1128/JB.175.24.7848-7855.1993
pubmed: 8253674
pmcid: 206961
Eriksson, J. M. & Haggård-Ljungquist, E. The multifunctional bacteriophage P2 Cox protein requires oligomerization for biological activity. J. Bacteriol. 182, 6714–6723 (2000).
doi: 10.1128/JB.182.23.6714-6723.2000
pubmed: 11073917
pmcid: 111415
Dodd, I. B., Reed, M. R. & Egan, J. B. The Cro‐like Apl repressor of coliphage 186 is required for prophage excision and binds near the phage attachment site. Mol. Microbiol. 10, 1139–1150 (1993).
doi: 10.1111/j.1365-2958.1993.tb00983.x
pubmed: 7934863
Bolotin, A. et al. The complete genome sequence of the lactic acid bacterium lactococcus lactis ssp. lactis IL1403. Genome Res. 11, 731–753 (2001).
doi: 10.1101/gr.GR-1697R
pubmed: 11337471
pmcid: 311110
Gasson, M. J. Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing. J. Bacteriol. 154, 1–9 (1983).
doi: 10.1128/JB.154.1.1-9.1983
pubmed: 6403500
pmcid: 217423
Altschul, S. F. et al. Gapped BLAST and PSI-BLAST: A new generation of protein database search programs. Nucleic Acids Res. 25, 3389–3402 (1997).
doi: 10.1093/nar/25.17.3389
pubmed: 9254694
pmcid: 146917
Little, J. W. Autodigestion of lexA and phage lambda repressors. Proc. Natl. Acad. Sci. USA 81, 1375–1379 (1984).
doi: 10.1073/pnas.81.5.1375
pubmed: 6231641
Pedersen, M., Ligowska, M. & Hammer, K. Characterization of the CI repressor protein encoded by the temperate lactococcal phage TP901-1. J. Bacteriol. 192, 2102–2110 (2010).
doi: 10.1128/JB.01387-09
pubmed: 20118255
pmcid: 2849442
Hayes, F., Daly, C. & Fitzgerald, G. F. Identification of the Minimal Replicon of Lactococcus lactis subsp. lactis UC317 Plasmid pCI305. Appl. Environ. Microbiol. 56, 202–209 (1990).
doi: 10.1128/AEM.56.1.202-209.1990
pubmed: 16348092
pmcid: 183273
Brøndsted, L. & Hammer, K. Use of the integration elements encoded by the temperate lactococcal bacteriophage TP901-1 to obtain chromosomal single-copy transcriptional fusions in Lactococcus lactis. Appl. Environ. Microbiol. 65, 752–758 (1999).
doi: 10.1128/AEM.65.2.752-758.1999
pubmed: 9925612
pmcid: 91091
Johansen, A. H., Brøndsted, L. & Hammer, K. Identification of operator sites of the CI repressor of phage TP901-1: Evolutionary link to other phages. Virology 311, 144–156 (2003).
doi: 10.1016/S0042-6822(03)00169-7
pubmed: 12832212
Terzaghi, B. E. & Sandine, W. E. Improved medium for lactic streptococci and their bacteriophages. Appl. Microbiol. 29, 807–813 (1975).
doi: 10.1128/AEM.29.6.807-813.1975
pubmed: 16350018
pmcid: 187084
Bertani, G. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J. Bacteriol. 62, 293–300 (1951).
doi: 10.1128/JB.62.3.293-300.1951
pubmed: 14888646
pmcid: 386127