FtsZ dimerization in vivo.

G Di Lallo; D Anderluzzi; P Ghelardini; L Paolozzi

doi:10.1046/j.1365-2958.1999.01344.x

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PubMed · 10231484

FtsZ dimerization in vivo.

G Di Lallo·D Anderluzzi·P Ghelardini·L Paolozzi

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Abstract

A hybrid assay, based on the properties of the lambda repressor, was developed to detect FtsZ dimerization in Escherichia coli in vivo. A gene fusion comprising the N-terminal end of the lambda cI repressor gene and the complete E. coli ftsZ gene was constructed. The fused protein resulted in a functional lambda repressor and was able to complement the thermosensitive mutant ftsZ84. Using the same strategy, a series of 10 novel mutants of FtsZ that are unable to dimerize was selected, and a deletion analysis of the protein was carried out. Characterization of these mutants allowed the identification of three separate FtsZ portions: the N-terminal of about 150 amino acids; the C-terminal of about 60 amino acids, which corresponds to the less conserved portion of the protein; and a central region of about 150 residues. Mutants belonging to this region would define the dimerization domain of FtsZ.

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Bacterial Proteins Bacteriophage lambda Blotting, Western Cytoskeletal Proteins Dimerization Escherichia coli Gene Deletion Mutation Plasmids Polymerase Chain Reaction Recombinant Fusion Proteins Recombination, Genetic Journal Article Research Support, Non-U.S. Gov't

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G Di Lallo, D Anderluzzi, P Ghelardini, L Paolozzi. 1999. FtsZ dimerization in vivo.. https://doi.org/10.1046/j.1365-2958.1999.01344.x

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