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Microbiology 149 (2003), 3353-3359; DOI  10.1099/mic.0.26580-0
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Microbiology 149 (2003), 3353-3359; DOI  10.1099/mic.0.26580-0
© 2003 Society for General Microbiology

Use of a two-hybrid assay to study the assembly of a complex multicomponent protein machinery: bacterial septosome differentiation

G. Di Lallo1, M. Fagioli1, D. Barionovi1, P. Ghelardini2 and L. Paolozzi1

1 Dipartimento di Biologia, Università "Tor Vergata", Via della Ricerca Scientifica, I-00133 Rome, Italy
2 Istituto di Biologia e Patologia Molecolari del CNR, Rome, Italy

Correspondence
L. Paolozzi
Paolozzi{at}bio.uniroma2.it

The ability of each of the nine Escherichia coli division proteins (FtsZ, FtsA, ZipA, FtsK, FtsQ, FtsL, FtsW, FtsI, FtsN) to interact with itself and with each of the remaining eight proteins was studied in 43 possible combinations of protein pairs by the two-hybrid system previously developed by the authors' group. Once the presumed interactions between the division proteins were determined, a model showing their temporal sequence of assembly was developed. This model agrees with that developed by other authors, based on the co-localization sequence in the septum of the division proteins fused with GFP. In addition, this paper shows that the authors' assay, which has already proved to be very versatile in the study of prokaryotic and eukaryotic protein interaction, is also a powerful instrument for an in vivo study of the interaction and assembly of proteins, as in the case of septum division formation.

Abbreviations: GFP, green fluorescent protein




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