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Lookup NU author(s): Dr Victor Hernandez-RocamoraORCiD
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The effects of Kil peptide from bacteriophage lambda 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 lambda 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 midpoint 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'-[(alpha,beta)-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.
Author(s): Hernandez-Rocamora VM, Alfonso C, Margolin W, Zorrilla S, Rivas G
Publication type: Article
Publication status: Published
Journal: Journal of Biological Chemistry
Year: 2015
Volume: 290
Issue: 33
Pages: 20325-20335
Print publication date: 14/08/2015
Online publication date: 29/06/2015
Acceptance date: 01/01/1900
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology
URL: http://dx.doi.org/10.1074/jbc.M115.653329
DOI: 10.1074/jbc.M115.653329
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