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Developing a method for systematic determination of FtsZ binding sites by NMR

Grant number: 13/26897-7
Support type:Scholarships abroad - Research Internship - Post-doctor
Effective date (Start): March 20, 2014
Effective date (End): March 19, 2015
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal researcher:Frederico José Gueiros Filho
Grantee:Patrícia Castellen
Supervisor abroad: Jose Manuel Andreu
Home Institution: Instituto de Química (IQ). Universidade de São Paulo (USP). São Paulo , SP, Brazil
Research place: Centro de Investigaciones Biológicas (CIB), Spain  


Bacterial cytokinesis is initiated by the polymerization of FtsZ, to form filaments with a repeating arrangement of subunits, connected head-to-tail. The assembly of FtsZ filaments around the longitudinal midpoint of the cell originates the Z-ring, a citoskeletal structure that serves as a scaffold for the bacterial division machine. As bacterial proteins involved in cell division are different from the eukaryotic cytoskeletal machinery, they have been recognized as good targets for new antibiotics. FtsZ, is a particularly good target because of its central role in division and because it interacts with a large array of modulatory proteins. To better understand the mechanism of Z ring formation and to characterize the mode of action of promising bioactive compounds, many efforts have been made to identify the specific interaction sites for modulatory proteins and small molecules in FtsZ. Thus, the present project proposes to create a new method to promptly map FtsZ interactions using NMR. (AU)

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
HUECAS, SONIA; RAMIREZ-APORTELA, ERNEY; VERGONOS, ALBERT; NUNEZ-RAMIREZ, RAFAEL; LLORCA, OSCAR; FERNANDO DIAZ, J.; JUAN-RODRIGUEZ, DAVID; OLIVA, MARIA A.; CASTELLEN, PATRICIA; ANDREU, JOSE M.. Self-Organization of FtsZ Polymers in Solution Reveals Spacer Role of the Disordered C-Terminal Tail. BIOPHYSICAL JOURNAL, v. 113, n. 8, p. 1831-1844, . (13/26897-7)

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