Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 19, Issue 10, Pages -Publisher
MDPI
DOI: 10.3390/ijms19102928
Keywords
cell division; Z associated protein A (ZapA); Filamenting temperature sensitive Z (FtsZ); quadrupole time of flight mass spectrometer (QTOF); Fourier-Transform Ion Cyclotron Resonance mass spectrometry(FTICR); 1,4-bis(succimidyl)-3-azidomethylglutarate (BAMG)
Funding
- DIVINOCELL project of the European Commission [FP7-Health-2007-B-223431]
- NWO, ALW open program [822.02.019]
- Higher Education Commission of the Royal Thai Government
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Cell division in bacteria is initiated by the polymerization of FtsZ at midcell in a ring-like structure called the Z-ring. ZapA and other proteins assist Z-ring formation and ZapA binds ZapB, which senses the presence of the nucleoids. The FtsZ-ZapA binding interface was analyzed by chemical cross-linking mass spectrometry (CXMS) under in vitro FtsZ-polymerizing conditions in the presence of GTP. Amino acids residue K42 from ZapA was cross-linked to amino acid residues K51 and K66 from FtsZ, close to the interphase between FtsZ molecules in protofilaments. Five different cross-links confirmed the tetrameric structure of ZapA. A number of FtsZ cross-links suggests that its C-terminal domain of 55 residues, thought to be largely disordered, has a limited freedom to move in space. Site-directed mutagenesis of ZapA reveals an interaction site in the globular head of the protein close to K42. Using the information on the cross-links and the mutants that lost the ability to interact with FtsZ, a model of the FtsZ protofilament-ZapA tetramer complex was obtained by information-driven docking with the HADDOCK2.2 webserver.
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