Structural and Functional Comparison Between the Stability Systems ParD of Plasmid R1 and Ccd of Plasmid F
Overview
Molecular Biology
Affiliations
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.
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.
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.
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.