Monitoring the flagella motor of plesiomonas shigelloides
- Autores: Zoha Tavakkoliamol
- Directores de la Tesis: Joan Tomás i Magaña (dir. tes.), Susana Merino Montero (dir. tes.)
- Lectura: En la Universitat de Barcelona ( España ) en 2021
- Idioma: español
- Tribunal Calificador de la Tesis: Núria Prim Bosch (presid.), Elena de Mendoza Barberá (secret.), Gabriel Forn Cuni (voc.)
- Programa de doctorado: Programa de Doctorado en Biotecnología por la Universidad de Barcelona
- Materias:
- Enlaces
- Tesis en acceso abierto en: TESEO
- Resumen
Plesiomonas shigelloides is the unique member of the Enterobacteriaceaefamily able to produce polar flagella when grow in liquid medium and lateral flagella when grown in solid or semisolid media. Two different gene clusters was found in P. shigelloides 302-73 strain, we found, one exclusively for the lateral flagella biosynthesis and the other one containing the biosynthetic polar flagella genes with additional putative glycosylation genes. Genes involved in the formation of the lophotricous flagella motor stator are not present in the two regions (regions I and II) involved in the biosynthesis of P. shigelloides lophotrichous flagella. In order to study of P. shigelloides genes which are involved in lophotricous and lateral flagella motor as well as their rotator energy source, we made different mutant unable to form the constitutive lophotrichous flagella. We analyzed rotation of lophotrichous and lateral flagella after treatment with different concentrations of amiloride and sodium chloride. Analysis of mutation of 302-73ΔmotX, 302-73ΔpomA1, 302-73ΔpomA2, 302-73ΔpomB1 and 302-73ΔpomB2, 302-73Δmaf-5ΔpomA1, 302-73Δmaf-5ΔpomA2, 302-73Δmaf-5ΔpomB1 and 302-73Δmaf-5 ΔpomB2 was done. The results suggested that PomA1, PomA2, PomB1 or PomB2 could be redundant pairs of stator-motor proteins which absence of one of them doesn't effect on lophotrichous flagella motility because they can compensation the lack of each other. The in-frame deletions mutants of 302-73ΔpomA2ΔpomB2, 302 73ΔpomA1ΔpomA2 and 302-73ΔpomB1ΔpomB2 indicated that pomA and pomB can be redundant proteins in P. Shigelloides. This result suggested that pomA1 pomB1 stator motor proteins are able to make an ion channel to circulate ion to the rotation of lophotrichous flagella. Mutants of 302-73Δ pomA2ΔpomB1 and 302-73Δ pomA1ΔpomB2, 302-73Δmaf-5Δ pomA2ΔpomB1 and 302-73Δmaf-5Δ pomA1ΔpomB2 showed replace of homologous stator motor proteins of P. Shigelloides are not predestined. Analyses of the FlgT protein function in the P. shigelloides motility was done by constructing mutation in flgT gene and motility assay was investigated in liquid and semi-solid plates in P. shigelloide 302-73 and the 302-73ΔflgT mutant. The data demonstrated that FlgT protein is not essential for anchoring the lophotricus or lateral flagella in P. Shigelloides surface. FlgT is present in the HBB of the unsheathed polar flagellum of P. shigelloide, sodium-driven by two different stator complexes, and this protein establishes a substructure in the polar HBB, H-ring, which is attached to the LP-ring and it is probably essential for anchorage and stability of the T-ring.
