Backbone and side chain NMR assignments of Geobacillus stearothermophilus ZapA allow identification of residues that mediate the interaction of ZapA with FtsZ

Author(s)

Nogueira, Maria Luiza C. ^[1] ; Sforca, Mauricio Luis ^[1] ; Chin, Yanni K. -Y. ^[2] ; Mobli, Mehdi ^[3] ; Handler, Aaron ^[4] ; Gorbatyuk, Vitaliy Y. ^[5] ; Robson, Scott A. ^[6] ; King, Glenn F. ^[2] ; Gueiros-Filho, Frederico J. ^[7] ; de Mattos Zeri, Ana Carolina ^[1]

Affiliation

^[1] Brazilian Biosci Natl Lab LNBio CNPEM, Campinas - Brazil

^[2] Univ Queensland, Inst Mol Biosci, Brisbane, Qld - Australia

^[3] Univ Queensland, Ctr Adv Imaging, Brisbane, Qld - Australia

^[4] Genzyme Sanofi US, Bioanalyt Sci DSAR Clin Lab Sci, Framingham, MA - USA

^[5] Univ Connecticut, BioNMR Facil, Biotechnol Bioserv Ctr, Mansfield, CT - USA

^[6] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 - USA

^[7] Univ Sao Paulo, Dept Bioquim, IQ, Sao Paulo - Brazil

• Document type: Journal article
• Source: BIOMOLECULAR NMR ASSIGNMENTS; v. 9, n. 2, p. 387-391, OCT 2015.
• Web of Science Citations: 1

Abstract

Bacterial division begins with the formation of a contractile protein ring at midcell, which constricts the bacterial envelope to generate two daughter cells. The central component of the division ring is FtsZ, a tubulin-like protein capable of self-assembling into filaments which further associate into a higher order structure known as the Z ring. Proteins that bind to FtsZ play a crucial role in the formation and regulation of the Z ring. One such protein is ZapA, a widely conserved 21 kDa homodimeric protein that associates with FtsZ filaments and promotes their bundling. Although ZapA was discovered more than a decade ago, the structural details of its interaction with FtsZ remain unknown. In this work, backbone and side chain NMR assignments for the Geobacillus stearothermophilus ZapA homodimer are described. We titrated FtsZ into (NH)-N-15-H-2-ZapA and mapped ZapA residues whose resonances are perturbed upon FtsZ binding. This information provides a structural understanding of the interaction between FtsZ and ZapA. (AU)

• FAPESP's process: 12/24916-1 - Structural studies of the Bacillus stearothermophilus's ZapA protein
• Grantee: Maria Luiza Caldas Nogueira
• Support type: Scholarships abroad - Research Internship - Doctorate
• FAPESP's process: 10/51866-0 - SMolBNet 2.0: combining genetics and NMR to dissect fundamental protein-protein interactions for complex bacterial division
• Grantee: Frederico José Gueiros Filho
• Support type: Regular Research Grants
• FAPESP's process: 12/15123-8 - Functional and structural characterization of the Bacillus's ZapA protein
• Grantee: Maria Luiza Caldas Nogueira
• Support type: Scholarships in Brazil - Doctorate