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

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. and de Mattos Zeri, Ana Carolina (2015) 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, 9 2: 387-391. doi:10.1007/s12104-015-9615-1


Author 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
Title Backbone and side chain NMR assignments of Geobacillus stearothermophilus ZapA allow identification of residues that mediate the interaction of ZapA with FtsZ
Formatted title
Backbone and side chain NMR assignments of Geobacillus stearothermophilus ZapA allow identification of residues that mediate the interaction of ZapA with FtsZ
Journal name Biomolecular NMR Assignments   Check publisher's open access policy
ISSN 1874-270X
1874-2718
Publication date 2015-05-13
Sub-type Article (original research)
DOI 10.1007/s12104-015-9615-1
Volume 9
Issue 2
Start page 387
End page 391
Total pages 5
Place of publication Dordrecht, Netherlands
Publisher Kluwer Academic Publishers
Collection year 2016
Language eng
Formatted 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 15N2H-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.
Keyword Bacterial cell division
FtsZ
ZapA
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2016 Collection
Institute for Molecular Bioscience - Publications
Centre for Advanced Imaging Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 1 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 0 times in Scopus Article
Google Scholar Search Google Scholar
Created: Tue, 02 Jun 2015, 10:13:06 EST by System User on behalf of Centre for Advanced Imaging