Structural studies of the Bacillus stearothermophilus's ZapA protein

• Grant number: 12/24916-1
• Support Opportunities: Scholarships abroad - Research Internship - Doctorate
• Effective date (Start): May 01, 2013
• Effective date (End): October 31, 2013
• Field of knowledge: Biological Sciences - Biochemistry - Chemistry of Macromolecules
• Principal Investigator: Ana Carolina de Mattos Zeri
• Grantee: Maria Luiza Caldas Nogueira
• Supervisor: Glenn F. King
• Host Institution: Centro Nacional de Pesquisa em Energia e Materiais (CNPEM). Ministério da Ciência, Tecnologia e Inovações (Brasil). Campinas , SP, Brazil
• Research place: University of Queensland, Brisbane (UQ), Australia
• Associated to the scholarship: 12/15123-8 - Functional and structural characterization of the Bacillus's ZapA protein, BP.DR

Abstract

The bacterial division occurs through a citocinetic apparatus that shrinks, resulting in two daughter cells. This apparatus, also known as divisome, is a macromolecular complex responsible for the change in growth direction of the bacterial envelope (membrane and cell wall), creating the division septum. A key step in the division is the Z-ring formation, a prokaryotic tubulin polymer, FtsZ, which surrounds the cell membrane forming a ring in the central cell. Once this ring is formed, it recruits other important proteins for the cell division, establishing functional divisomes. It is known that there are two major groups of protein comprising the divisome, the first group is responsible for cell wall synthesis, which form the split septum, and the last group modulates the dynamics of the Z ring through the spatio-temporal regulation of its formation. This group is divided between positive and negative modulatory proteins, which act aiding or inhibiting, respectively, the formation of the ring Z. The ZapA protein (Z ring associated protein A), is a positive modulator by assisting the polymerization of FtsZ and stabilize the interaction between the formed protofilaments of the protein polymers. It promotes lateral association of FtsZ filaments by helping with the continuous ring formation of relatively short polymers. Our aim is to characterize the ZapA structure in order to understand its function and to analyze their interaction with FtsZ protein to unravel molecular mechanisms of interaction between those proteins. (AU)

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)

NOGUEIRA, MARIA LUIZA C.; SFORCA, MAURICIO LUIS; CHIN, YANNI K. -Y.; MOBLI, MEHDI; HANDLER, AARON; GORBATYUK, VITALIY Y.; ROBSON, SCOTT A.; KING, GLENN F.; GUEIROS-FILHO, FREDERICO J.; DE MATTOS ZERI, ANA CAROLINA. Backbone and side chain NMR assignments of Geobacillus stearothermophilus ZapA allow identification of residues that mediate the interaction of ZapA with FtsZ. BIOMOLECULAR NMR ASSIGNMENTS, v. 9, n. 2, p. 387-391, OCT 2015. (12/15123-8, 12/24916-1, 10/51866-0)