Phage-display and correlated mutations identify an essential region of subdomain 1C involved in homodimerization of XXXX FtsA.

@entity855 @entity1522 @entity526
FtsA plays an essential role in @entity526 cell division and is nearly ubiquitous in eubacteria. Several evidences postulated the ability of FtsA to interact with other septation proteins and with itself. To investigate these binding properties, we screened a phage-display library with FtsA. The isolated peptides defined a degenerate consensus sequence, which in turn displayed a striking similarity with residues 126-133 of FtsA itself. This result suggested that residues 126-133 were involved in homodimerization of FtsA. The hypothesis was supported by the analysis of correlated mutations, which identified a mutual relationship between a group of @entity1522 encompassing the @entity855 -binding site and a set of residues immediately downstream to @entity1522 126-133. This information was used to assemble a model of a FtsA homodimer, whose accuracy was confirmed by probing multiple alternative docking solutions. Moreover, a prediction of residues responsible for protein-protein interaction validated the proposed model and confirmed once more the importance of residues 126-133 for homodimerization. To functionally characterize this region, we introduced a deletion in ftsA, where residues 126-133 were skipped. This mutant failed to complement conditional lethal alleles of ftsA, demonstrating that @entity1522 126-133 play an essential role in @entity526 .
