Functional analysis of predicted coiled-coil regions in the Escherichia coli K-12 O-antigen polysaccharide chain length determinant Wzz.

Journal of Bacteriology
Cristina L MaroldaMiguel A Valvano

Abstract

Wzz is a membrane protein that determines the chain length distribution of the O-antigen lipopolysaccharide by an unknown mechanism. Wzz proteins consist of two transmembrane helices separated by a large periplasmic loop. The periplasmic loop of Escherichia coli K-12 Wzz (244 amino acids from K65 to A308) was purified and found to be a monomer with an extended conformation, as determined by gel filtration chromatography and analytical ultracentrifugation. Circular dichroism showed that the loop has a 60% helical content. The Wzz periplasmic loop also contains three regions with predicted coiled coils. To probe the function of the predicted coiled coils, we constructed amino acid replacement mutants of the E. coli K-12 Wzz protein, which were designed so that the coiled coils could be separate without compromising the helicity of the individual molecules. Mutations in one of the regions, spanning amino acids 108 to 130 (region I), were associated with a partial defect in O-antigen chain length distribution, while mutants with mutations in the region spanning amino acids 209 to 223 (region III) did not have an apparent functional defect. In contrast, mutations in the region spanning amino acids 153 to 173 (region II) eliminated t...Continue Reading

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Citations

Apr 15, 2008·Journal of Bacteriology·Natalia JimenezJuan M Tomás
Mar 29, 2013·Future Microbiology·Biao YuanMingshu Wang
Dec 9, 2008·Trends in Biochemical Sciences·Renato MoronaMiroslaw Cygler
Aug 19, 2008·FEMS Microbiology Letters·Monica M Cunneen, Peter R Reeves

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