FtsZ dimerization in vivo.
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.
Di Lallo
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Dipartimento di Biologia, Università di Roma 'Tor Vergata', via della Ricerca Scientifica, La Romanina, Rome, Italy.
Anderluzzi
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D
Ghelardini
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Paolozzi
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D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D010582:Bacteriophage lambda / Q000502:physiology; D015153:Blotting, Western; D003598:Cytoskeletal Proteins; D019281:Dimerization; D004926:Escherichia coli / Q000254:growth & development / Q000378:metabolism* / Q000821:virology; D017353:Gene Deletion; D009154:Mutation; D010957:Plasmids / Q000235:genetics; D016133:Polymerase Chain Reaction / Q000379:methods; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D011995:Recombination, Genetic
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D011993:Recombinant Fusion Proteins