title: Backbone and side chain NMR assignments of Geobacillus stearothermophilus ZapA allow identification of residues that mediate the interaction of ZapA with FtsZ.
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 (15)N(2)H-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.
authors.affiliation: Brazilian Biosciences National Laboratory (LNBio-CNPEM), Campinas, Brazil. marialuiza.nogueira@lnbio.cnpem.br.
authors.forename: Maria Luiza C
authors.initials: ML
authors.lastname: Nogueira
authors.affiliation: Brazilian Biosciences National Laboratory (LNBio-CNPEM), Campinas, Brazil.
authors.forename: Mauricio Luis
authors.initials: ML
authors.lastname: Sforça
authors.affiliation: Institute for Molecular Bioscience, The University of Queensland, Brisbane, Australia.
authors.forename: Yanni K-Y
authors.initials: YK
authors.lastname: Chin
authors.affiliation: Centre for Advanced Imaging, The University of Queensland, Brisbane, Australia.
authors.forename: Mehdi
authors.initials: M
authors.lastname: Mobli
authors.affiliation: Bioanalytical Sciences DSAR Clinical Laboratory Sciences, Genzyme/Sanofi US, Framingham, MA, USA.
authors.forename: Aaron
authors.initials: A
authors.lastname: Handler
authors.affiliation: BioNMR Facility, Biotechnology-Bioservices Center, University of Connecticut, Mansfield, CT, USA.
authors.forename: Vitaliy Y
authors.initials: VY
authors.lastname: Gorbatyuk
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, USA.
authors.forename: Scott A
authors.initials: SA
authors.lastname: Robson
authors.affiliation: Institute for Molecular Bioscience, The University of Queensland, Brisbane, Australia.
authors.forename: Glenn F
authors.initials: GF
authors.lastname: King
authors.affiliation: Departamento de Bioquímica, IQ, Universidade de São Paulo, São Paulo, Brazil. fgueiros@iq.usp.br.
authors.forename: Frederico J
authors.initials: FJ
authors.lastname: Gueiros-Filho
authors.affiliation: Brazilian Biosciences National Laboratory (LNBio-CNPEM), Campinas, Brazil. ana.zeri@lnbio.cnpem.br.
authors.forename: Ana Carolina de Mattos
authors.initials: AC
authors.lastname: Zeri
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D001411:Geobacillus stearothermophilus / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D066244:Proton Magnetic Resonance Spectroscopy
chemical_list: D000596:Amino Acids; D001426:Bacterial Proteins
keywords: Bacterial cell division; FtsZ; ZapA