Oligomerization of FtsZ Converts the FtsZ Tail Motif (CCTP) into a Multivalent Ligand with High Avidity for Partners ZipA and SlmA

Du S, Park K, Lutkenhaus J, 95(2):173-88, Mol Microbiol, 2015

Described herein is an investigation to differentiate affinities between ZipA binding to full-length FtsZ versus a short peptide located at the carboxy terminus of FtsZ, referred to as the CCTP (conserved carboxy-terminal peptide). The interaction of SlmA and FtsZ was also evaluated. A series of Bio-Layer Interferometry assays performed using a Pall ForteBio BLItz instrument equipped with Ni-NTA biosensors. Thereby binding of FtsZ, FtsZ mutants, MalE-CCTP, or MinDΔ10-linker-CCTP to His tagged ZipA were studied. In a reciprocal binding evaluation, His-FtsZ was captured on to Ni-NTA biosensors and binding to untagged ZipA was analyzed. In the assays with SlmA, the His-SlmA/SBS complexes were loaded on to Ni-NTA Biosensor tips and binding of FtsZ, FtsZ mutants, or MinDΔ10-linker-CCTP was tested. Overall results suggest that the oligomerization of FtsZ is important for the enhanced affinity of FtsZ towards ligands that bind the CCTP.

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