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FtsZ dimerization in vivo
Author(s) -
Di Lallo G.,
Anderluzzi D.,
Ghelardini P.,
Paolozzi L.
Publication year - 1999
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1999.01344.x
Subject(s) - ftsz , mutant , biology , repressor , escherichia coli , gene , fusion protein , microbiology and biotechnology , genetics , biochemistry , recombinant dna , gene expression
A hybrid assay, based on the properties of the λ repressor, was developed to detect FtsZ dimerization in Escherichia coli in vivo . A gene fusion comprising the N‐terminal end of the λ cI repressor gene and the complete E. coli ftsZ gene was constructed. The fused protein resulted in a functional λ repressor and was able to complement the thermosensitive mutant ftsZ 84 . 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.