RESUMEN
The SulA protein of Escherichia coli and related bacteria interacts directly with FtsZ, blocking cell division by disrupting Z-ring formation, yet the precise mechanism remains not fully understood. Previous demonstrations of Pseudomonas aeruginosa SulA's dimerization capability were confined to X-ray crystallography and lacked confirmation under in vivo conditions. Additionally, uncertainty persisted regarding the dimerization potential of E. coli's SulA protein. This paper employs a bacterial two-hybrid system to establish that both P. aeruginosa and E. coli SulA proteins indeed possess the capacity for dimerization.
Asunto(s)
Proteínas de Escherichia coli , Escherichia coli , Escherichia coli/metabolismo , Pseudomonas aeruginosa , Proteínas Bacterianas/química , Dimerización , Proteínas de Escherichia coli/metabolismo , División CelularRESUMEN
SOS-response is an important tool of bacteria intended to protect their genome and thereby allow them to survive under adverse conditions. Recently SOS-response is considered to enhance mutagenesis and thus help bacteria acquire antibiotic resistance. Due to high significance of this phenomena it seems to be important to investigate processes that allow bacteria to survive after SOS-response activation. In current work the recovery of division process of Escherichia coli cells after division arrest due to expression of SOS-response protein SulA was studied. Data indicate that cells are able to rapidly restore normal division; also nucleoid occlusion seems to be the main septum positioning mechanism during the process. In the course of recovery FtsZ forms helix-like structures, which then transformate into Z-rings.
Asunto(s)
Proteínas Bacterianas/metabolismo , Citocinesis/fisiología , Proteínas del Citoesqueleto/metabolismo , Proteínas de Escherichia coli/metabolismo , Escherichia coli/metabolismo , Respuesta SOS en Genética/fisiología , Proteínas Bacterianas/genética , Proteínas del Citoesqueleto/genética , Escherichia coli/genética , Proteínas de Escherichia coli/genéticaRESUMEN
FtsZ--a bacterial tubulin homolog--is one of the key bacterial division proteins, forming a contractile Z-ring at the midcell of dividing bacteria. In this work immunofluorescent labeling was used in conjunction with single-molecule localization microscopy (SMLM) to visualize native structures formed by FtsZ protein in Escherichia coli cells. This approach allowed the reorganization of FtsZ structures during cytokinesis to be visualized step-by-step. New data was obtained that support the hypothesis that the Z-ring is a spiral structure that constricts during division, assisting the formation of the septum between daughter cells.