Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria - PubMed (original) (raw)
Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria
L Van Melderen et al. Mol Microbiol. 1994 Mar.
Abstract
The ccd locus contributes to the stability of plasmid F by post-segregational killing of plasmid-free bacteria. The ccdB gene product is a potent cell-killing protein and its activity is negatively regulated by the CcdA protein. In this paper, we show that the CcdA protein is unstable and that the degradation of CcdA is dependent on the Lon protease. Differences in the stability of the killer CcdB protein and its antidote CcdA are the key to post-segregational killing. Because the half-life of active CcdA protein is shorter than that of active CcdB protein, persistence of the CcdB protein leads to the death of plasmid-free bacterial segregants.
Similar articles
- ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions.
Van Melderen L, Thi MH, Lecchi P, Gottesman S, Couturier M, Maurizi MR. Van Melderen L, et al. J Biol Chem. 1996 Nov 1;271(44):27730-8. doi: 10.1074/jbc.271.44.27730. J Biol Chem. 1996. PMID: 8910366 - Efficiency of the pTF-FC2 pas poison-antidote stability system in Escherichia coli is affected by the host strain, and antidote degradation requires the lon protease.
Smith AS, Rawlings DE. Smith AS, et al. J Bacteriol. 1998 Oct;180(20):5458-62. doi: 10.1128/JB.180.20.5458-5462.1998. J Bacteriol. 1998. PMID: 9765581 Free PMC article. - The ratio between CcdA and CcdB modulates the transcriptional repression of the ccd poison-antidote system.
Afif H, Allali N, Couturier M, Van Melderen L. Afif H, et al. Mol Microbiol. 2001 Jul;41(1):73-82. doi: 10.1046/j.1365-2958.2001.02492.x. Mol Microbiol. 2001. PMID: 11454201 - Molecular interactions of the CcdB poison with its bacterial target, the DNA gyrase.
Van Melderen L. Van Melderen L. Int J Med Microbiol. 2002 Feb;291(6-7):537-44. doi: 10.1078/1438-4221-00164. Int J Med Microbiol. 2002. PMID: 11890555 Review. - [Structural and functional characteristics of ATP-dependent Lon-proteinase from Escherichia coli].
Rotanova TV. Rotanova TV. Bioorg Khim. 1999 Dec;25(12):883-91. Bioorg Khim. 1999. PMID: 10734549 Review. Russian.
Cited by
- Characterization of the phd-doc and ccd toxin-antitoxin cassettes from Vibrio superintegrons.
Guérout AM, Iqbal N, Mine N, Ducos-Galand M, Van Melderen L, Mazel D. Guérout AM, et al. J Bacteriol. 2013 May;195(10):2270-83. doi: 10.1128/JB.01389-12. Epub 2013 Mar 8. J Bacteriol. 2013. PMID: 23475970 Free PMC article. - Assembly dynamics and stability of the pneumococcal epsilon zeta antitoxin toxin (PezAT) system from Streptococcus pneumoniae.
Mutschler H, Reinstein J, Meinhart A. Mutschler H, et al. J Biol Chem. 2010 Jul 9;285(28):21797-806. doi: 10.1074/jbc.M110.126250. Epub 2010 May 4. J Biol Chem. 2010. PMID: 20442221 Free PMC article. - Crystal structure of toxin HP0892 from Helicobacter pylori with two Zn(II) at 1.8 Å resolution.
Im H, Jang SB, Pathak C, Yang YJ, Yoon HJ, Yu TK, Suh JY, Lee BJ. Im H, et al. Protein Sci. 2014 Jun;23(6):819-32. doi: 10.1002/pro.2465. Epub 2014 Apr 15. Protein Sci. 2014. PMID: 24677509 Free PMC article. - Chromosomal toxin-antitoxin systems may act as antiaddiction modules.
Saavedra De Bast M, Mine N, Van Melderen L. Saavedra De Bast M, et al. J Bacteriol. 2008 Jul;190(13):4603-9. doi: 10.1128/JB.00357-08. Epub 2008 Apr 25. J Bacteriol. 2008. PMID: 18441063 Free PMC article. - Expression of different ParE toxins results in conserved phenotypes with distinguishable classes of toxicity.
Ames JR, Muthuramalingam M, Murphy T, Najar FZ, Bourne CR. Ames JR, et al. Microbiologyopen. 2019 Oct;8(10):e902. doi: 10.1002/mbo3.902. Epub 2019 Jul 16. Microbiologyopen. 2019. PMID: 31309747 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases