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Targetting assembly of cell division protein FtsZ with small molecules

AuthorsSchaffner-Barbero, Claudia ; Martín-Fontecha, Mar; Chacón, Pablo ; Andreu, José Manuel
Issue Date2012
PublisherAmerican Chemical Society
CitationACS Chemical Biology 7(2):269-277(2012)
AbstractFtsZ is the key protein of bacterial cell division and an emergent target for new antibiotics. It is a filament-forming GTPase and a structural homologue of eukaryotic tubulin. A number of FtsZ-interacting compounds have been reported, some of which have powerful antibacterial activity. Here we review recent advances and new approaches in modulating FtsZ assembly with small molecules. This includes analyzing their chemical features, binding sites, mechanisms of action, the methods employed, and computational insights, aimed at a better understanding of their molecular recognition by FtsZ and at rational antibiotic design. Cell division protein FtsZ is employed by most bacteria to divide. It forms the cytokinetic Z-ring at the division site(1) (Figure 1), is tethered to the inner face of the plasma membrane by FtsA and ZipA, and recruits other accessory proteins of the cell division machinery (divisome), several of which are essential for remodeling the cell wall peptidoglycan at the septum.(2, 3) The assembly of the Z-ring is coordinated with DNA segregation and cell growth through many regulatory proteins in different bacteria.(2) The bacterial division proteins differ from the proteins of eukaryotic cytokinesis. Thus, bacterial cytoskeleton and cell division have been recognized as attractive targets for seeking new antibiotics(4, 5) with which to fight the widespread emergence of pathogens resistant to current antibiotics.(6) FtsZ has been validated as a target for antibacterial intervention with a synthetic compound active on an in vivo model of infection.(7) Very recently, it has been found that antibiotic acyldepsipeptides activate bacterial ClpP peptidase to degrade FtsZ.(8) Here we review small molecule approaches for targeting FtsZ assembly
Description9 páginas, 4 figuras, 1 tabla -- PAGS nros. 269-277
Publisher version (URL)http://dx.doi.org/ 10.1021/cb2003626
Appears in Collections:(CIB) Artículos
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