The division machinery of Eubacteria is made through the formation of a macromolecular complex containing at least twelve proteins, which assemble with a defined dependence hierarchy at the site of division. The organization of the genes coding for division proteins is generally conserved, despite the low sequence homology, and in many different bacteria, including Gram-negative and Gram-positive rods or cocci, the major proteins involved in the division process appear to be conserved. In particular, at least eight proteins are present in almost all cell wall containing Eubacteria: FtsZ, FtsA FtsK, FtsQ/DivIB, DivIC/FtsB, FtsL, FtsW and FtsI, although additional proteins may also be present, depending on the bacterial species. The ability of each of the eleven E. coli and Streptococcus pneumoniae division proteins to interact with itself and with each of the remaining proteins was studied in all the possible combinations of protein pairs, using a bacterial two-hybrid system and co-immune precipitation experiments. Then, comparison between the S. pneumoniae division protein interaction web and that of E. coli, was performed. At least 9 division proteins, ZapA, FtsZ, FtsA, FtsK, FtsQ/DivIB, FtsB/DivIC, FtsL, FtsI, FtsW are believed to have a conserved function between these bacteria and thus we may say that a significant part of the interactions were conserved. Out of 45 protein pairs tested for each bacterium, 30 showed the same behavior: 23 interacted while 7 did not. In agreement with these results, cross-interactions between S. pneumoniae proteins with the corresponding E. coli orthologs were observed. Taken together, these results suggest a phylogenetically conserved minimal common interactome of the division proteins. Biotechnological applications of these results could be the identification of new bacterial targets, both of broad and specie-specific host range, for a novel antimicrobial class inhibiting the protein-protein interaction.
A prokaryotic minimal common interactome of the division proteins: a new perspective for novel antibacterial drugs
Ghelardini P;
2009
Abstract
The division machinery of Eubacteria is made through the formation of a macromolecular complex containing at least twelve proteins, which assemble with a defined dependence hierarchy at the site of division. The organization of the genes coding for division proteins is generally conserved, despite the low sequence homology, and in many different bacteria, including Gram-negative and Gram-positive rods or cocci, the major proteins involved in the division process appear to be conserved. In particular, at least eight proteins are present in almost all cell wall containing Eubacteria: FtsZ, FtsA FtsK, FtsQ/DivIB, DivIC/FtsB, FtsL, FtsW and FtsI, although additional proteins may also be present, depending on the bacterial species. The ability of each of the eleven E. coli and Streptococcus pneumoniae division proteins to interact with itself and with each of the remaining proteins was studied in all the possible combinations of protein pairs, using a bacterial two-hybrid system and co-immune precipitation experiments. Then, comparison between the S. pneumoniae division protein interaction web and that of E. coli, was performed. At least 9 division proteins, ZapA, FtsZ, FtsA, FtsK, FtsQ/DivIB, FtsB/DivIC, FtsL, FtsI, FtsW are believed to have a conserved function between these bacteria and thus we may say that a significant part of the interactions were conserved. Out of 45 protein pairs tested for each bacterium, 30 showed the same behavior: 23 interacted while 7 did not. In agreement with these results, cross-interactions between S. pneumoniae proteins with the corresponding E. coli orthologs were observed. Taken together, these results suggest a phylogenetically conserved minimal common interactome of the division proteins. Biotechnological applications of these results could be the identification of new bacterial targets, both of broad and specie-specific host range, for a novel antimicrobial class inhibiting the protein-protein interaction.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
