» Articles » PMID: 2017133

Structural and Functional Comparison Between the Stability Systems ParD of Plasmid R1 and Ccd of Plasmid F

Overview
Journal Mol Gen Genet
Date 1991 Mar 1
PMID 2017133
Citations 7
Authors
Affiliations
Soon will be listed here.
Abstract

The stability determined by the systems ParD of plasmid R1 and Ccd of plasmid F is due to the concerted action of two proteins, a cytotoxin and an antagonist of this function. In this paper we report that CcdA and Kis proteins, the antagonists of the Ccd and ParD systems respectively, share significant sequence homologies at both ends. In Kis, these regions seem to correspond to two different domains. Despite the structural similarities, Kis and CcdA are not interchangeable. In addition we have shown that the cytotoxins of these systems, the Kid and CcdB proteins, do not share structural homologies. In contrast to CcdB, the Kid protein of the ParD system induces RecA-dependent cleavage of the cI repressor of bacteriophage lambda very inefficiently or not at all. The functional implications of these results are discussed.

Citing Articles

A common origin for the bacterial toxin-antitoxin systems parD and ccd, suggested by analyses of toxin/target and toxin/antitoxin interactions.

Smith A, Lopez-Villarejo J, Diago-Navarro E, Mitchenall L, Barendregt A, Heck A PLoS One. 2012; 7(9):e46499.

PMID: 23029540 PMC: 3460896. DOI: 10.1371/journal.pone.0046499.


The solution structure of ParD, the antidote of the ParDE toxin antitoxin module, provides the structural basis for DNA and toxin binding.

Oberer M, Zangger K, Gruber K, Keller W Protein Sci. 2007; 16(8):1676-88.

PMID: 17656583 PMC: 2203376. DOI: 10.1110/ps.062680707.


Modular organization of the Phd repressor/antitoxin protein.

Smith J, Magnuson R J Bacteriol. 2004; 186(9):2692-8.

PMID: 15090510 PMC: 387787. DOI: 10.1128/JB.186.9.2692-2698.2004.


The anti-toxin ParD of plasmid RK2 consists of two structurally distinct moieties and belongs to the ribbon-helix-helix family of DNA-binding proteins.

Oberer M, Zangger K, Prytulla S, Keller W Biochem J. 2001; 361(Pt 1):41-7.

PMID: 11743881 PMC: 1222296. DOI: 10.1042/0264-6021:3610041.


Toxin-antitoxin modules may regulate synthesis of macromolecules during nutritional stress.

Gerdes K J Bacteriol. 2000; 182(3):561-72.

PMID: 10633087 PMC: 94316. DOI: 10.1128/JB.182.3.561-572.2000.


References
1.
Miki T, Yoshioka K, Horiuchi T . Control of cell division by sex factor F in Escherichia coli. I. The 42.84-43.6 F segment couples cell division of the host bacteria with replication of plasmid DNA. J Mol Biol. 1984; 174(4):605-25. DOI: 10.1016/0022-2836(84)90086-x. View

2.
Hiraga S, Jaffe A, Ogura T, Mori H, Takahashi H . F plasmid ccd mechanism in Escherichia coli. J Bacteriol. 1986; 166(1):100-4. PMC: 214563. DOI: 10.1128/jb.166.1.100-104.1986. View

3.
Sweet R, Eisenberg D . Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structure. J Mol Biol. 1983; 171(4):479-88. DOI: 10.1016/0022-2836(83)90041-4. View

4.
Rose G, Geselowitz A, Lesser G, Lee R, Zehfus M . Hydrophobicity of amino acid residues in globular proteins. Science. 1985; 229(4716):834-8. DOI: 10.1126/science.4023714. View

5.
Brandenburger A, Bailone A, Levine A, Devoret R . Gratuitous induction. J Mol Biol. 1984; 179(3):571-6. DOI: 10.1016/0022-2836(84)90082-2. View