Genetic control of the cell cycle

Vicente

 

Miguel Vicente

Group Leader

Contact

Info about Divinocell Project

 

 Research summary

This group works to find inhibitable targets in essential bacterial functions, namely cell growth and division, with the purpose of designing assays to identify new antimicrobials. For this goal we study first the proliferation of a Gram-negative bacteria, Escherichia coli, in which both commensal and pathogenic strains exists.

 

Publications

Sánchez-Gorostiaga A, Palacios P, Martínez-Arteaga R, Sánchez M, Casanova M, Vicente M. Life without division: Physiology of Escherichia coli FtsZ-deprived filaments.Escherichia coli FtsZ-deprived filaments. mBio 2016; 7: e01620-16

Ortiz C, Natale P, Cueto L, Vicente M. The Keepers of the Ring: regulators of FtsZ assembly. FEMS Microbiol Rev 2016; 40: 57-67

Ortiz C, Kureisaite-Ciziene D, Schmit F, McLaughlin SH, Vicente M, Löwe J. Crystal structure of the Z-ring associated cell division protein ZapC from Escherichia coli.Escherichia coli. FEBS Lett 2015; 589: 3822–3828

Gola S, Munder T, Casonato S, Manganelli R. Vicente M. The essential role of SepF in mycobacterial division. Mol Microbiol 2015; 97: 560–576

Cabré EJ, Monterroso B, Alfonso C, Sánchez-Gorostiaga A, Reija B, Jiménez M, Vicente M*, Zorrilla S*, Rivas G*. The nucleoid occlusion SlmA protein accelerates the disassembly of the FtsZ polymers without affecting their GTPase activity. PLoS One 2015; 10: e0126434 (*equal contribution)

 

 

FtsZ, a GTPase found in the cytoplasm of most bacteria, is the major component of the machinery responsible for division (the divisome) in Escherichia coli. As well as forming polymers, it interacts with additional proteins that contribute to its function by forming a ring at the midcell that is essential to constrict the membrane. FtsZ is anchored indirectly to the membrane and is prevented from polymerizing at locations where septation is undesired. Several FtsZ properties are mediated by other proteins that function as keepers of the ring. ZipA and FtsA serve to anchor the ring, and together with a set of Zap proteins, they stabilize it. The MinCDE and SlmA proteins prevent polymerization of FtsZ at sites other than the midcell. ClpP degrades FtsZ, an action prevented by ZipA. Many of the FtsZ keepers interact with FtsZ through a central hub located at its carboxy terminal end.

Besides causing filamentation due to division arrest, the very low FtsZ levels in FtsZ-deprived cells have severe pleiotropic effects on E. coli physiology that compromise bacterial survival. In contrast to FtsZ-deprived cells, the viability of filaments formed by a conditional mutant is not affected when FtsZ activity is lost, because the amount of the protein remains unperturbed. We propose that the quest for new antimicrobials that target FtsZ should be directed to decreasing the number of FtsZ molecules rather than to inhibiting its activity.

The Mycobacteria include important human pathogens. The mycobacterial SepF homologue is highly conserved in the Mycobacterium tuberculosis complex. SepF is a key component of the mycobacterial divisome, necessary for division. It interacts with FtsZ and is located in a ring-like structure at potential division sites in an FtsZ-dependent manner, making it an attractive target for proliferation blockade.

 

figure1Vicentefigure2Vicente

 

grupoVicenteRed 

Name
Position
Contact
Miguel Vicente Principal investigator
Ana Isabel Rico Postdoctoral scientist
Susanne Gola Postdoctoral scientist
Alicia Sánchez Gorostiaga Postdoctoral scientist
Cristina Ortiz Predoctoral scientist
Laura Cueto Predoctoral scientist
Pilar Palacios Technicians
Mercedes Casanova Technicians

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