Combining Mass Spectrometry Cross‐Linking, Molecular Docking and NMR Titration to Dissect ZapA‐FtsZ Protein Interaction

• Published in: The FASEB journal 2016-04, Vol.30 (S1)
• Main Authors: Nogueira, Maria Luiza Caldas, Sforça, Mauricio Luis, Leme, Adriana Franco Paes, Pauletti, Bianca Alves, de Oliveira, Paulo Sergio Lopes, Honorato, Rodrigo Vargas, King, Glenn F, Filho, Frederico José Gueiros, de Mattos Zeri, Ana Carolina
• Format: Article
• Language: English
• ISSN: 0892-6638; 1530-6860
• DOI: 10.1096/fasebj.30.1_supplement.lb60

Abstract only The cell division is a key event in a bacteria cycle of life and in most rod shaped bacteria. This cell divion involves a septum formation. FtsZ and other proteins forms a macromolecular complex, named Divisome, which redirect the cell wall and provide a constrictive force required to divide the bacterial cell in two daughter cells. FtsZ is a tubulin homologue that polymerizes as a ring structure shaped, the Z ring. The Divisome is composed by: the Z ring, modulators proteins, proteins that anchor the Z ring to the cell membrane and synthesize cell wall (peptidoglycan). Modulators proteins are essential for the cell division occurs at the right place and time, because they act stimulating or preventing the Z ring formation. Defects on modular proteins could cause defects in bacterial cell division such as filamentation and mini‐cell formation. The Z ring associated protein A (ZapA) is a positive modulator that assists the bundling of FtsZ polymers by promote lateral association of FtsZ filaments. Despite the interaction between FtsZ‐ZapA was described many years ago, the molecular mechanisms details involved into this process is barely understood. Here we combined the information obtained from FtsZ‐ZapA NMR titration and Mass Spectrometry cross‐linking to modelling the FtsZ and ZapA protein complex. The docking model may give us a clue of the main amino acids residues involved on that interaction and how thus it occurs. Support or Funding Information São Paulo Research Foundation (FAPESP); State University of Campinas (UNICAMP) and Brazilian Center for Research in Energy and Materials/Brazilian Biosciences National Laboratory ( CNPEM/LNBio )