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Evidence that bacteriophage λ kil peptide inhibits bacterial cell division by disrupting FtsZ protofilaments and sequestering protein subunits

AuthorsHernández-Rocamora, V. M. ; Alfonso, Carlos ; Margolin, William; Zorrilla, Silvia ; Rivas, Germán
KeywordsEscherichia coli (E. coli)
Cell division
Protein-protein interaction
Issue Date29-Jun-2015
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJ Biol Chem.290(33):20325-35 (2015)
AbstractThe effects of Kil peptide from bacteriophage λ on the assembly of Escherichia coli FtsZ into one subunit thick protofilaments were studied using combined biophysical and biochemical methods. Kil peptide has recently been identified as the factor from bacteriophage λ responsible for the inhibition of bacterial cell division during lytic cycle, targeting FtsZ polymerization. Here, we show that this antagonist blocks FtsZ assembly into GTP-dependent protofilaments, producing a wide distribution of smaller oligomers compared with the average size of the intact protofilaments. The shortening of FtsZ protofilaments by Kil is detectable at concentrations of the peptide in the low micromolar range, the mid-point of the inhibition being close to its apparent affinity for GDP-bound FtsZ. This antagonist not only interferes with FtsZ assembly but also reverses the polymerization reaction. The negative regulation by Kil significantly reduces the GTPase activity of FtsZ protofilaments, and FtsZ polymers assembled in guanosine-5'-[(α,β)-methyleno]triphosphate are considerably less sensitive to Kil. Our results suggest that, at high concentrations, Kil may use an inhibition mechanism involving the sequestration of FtsZ subunits, similar to that described for other inhibitors like the SOS response protein SulA or the moonlighting enzyme OpgH. This mechanism is different from those employed by the division site selection antagonists MinC and SlmA. This work provides new insight into the inhibition of FtsZ assembly by phages, considered potential tools against bacterial infection.
Description11 p.-7 fig.
Publisher version (URL)http://dx.doi.org/ 10.1074/jbc.M115.653329
Appears in Collections:(CIB) Artículos
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