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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 383, Issue 11


In vitro and in vivo Stability of the 2ζ2 Protein Complex of the Broad Host-Range Streptococcus pyogenes pSM19035 Addiction System

A.G. Camacho / R. Misselwitz / J. Behlke / S. Ayora / K. Welfle / A. Meinhart / B. Lara / W. Saenger / H. Welfle / J.C. Alons
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.191


Streptococcus pyogenes pSM19035-encoded (10.7 kDa) and ζ (32.4 kDa) proteins are necessary to secure stable plasmid inheritance in bacteria, with ζ acting as toxin that kills plasmiddeprived cells and as an antitoxin that neutralises the activity of ζ. The and ζ proteins copurify as a stable complex that, according to analytical ultracentrifugation and gel filtration, exists as 2ζ2 heterotetramer in solution. Cocrystals of the 2ζ2 complex contain and ζ in 1:1 molar ratio. Unfolding studies monitoring circular dichroic and fluorescence changes show that the ζ protein has a significantly lower thermodynamic stability than the protein both in free state and in the complex. Proteolytic studies indicate that ζ protein is more stable in the the 2ζ2 complex than in the free state. In vivo studies reveal a short halflife of the antitoxin (~18min) and a long lifetime of the ζ toxin (>60min). When transcriptiontranslation of a plasmid containing the and ζ genes was inhibited, cell death was observed after a short lag phase that correlates with the disappearance of the protein from the background.

About the article

Published Online: 2005-06-01

Published in Print: 2002-11-13

Citation Information: Biological Chemistry, Volume 383, Issue 11, Pages 1701–1713, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.191.

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